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Information on EC 7.2.2.20 - ABC-type Zn2+ transporter
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7.2.2.20 ABC-type Zn2+ transporterIUBMB Comments
ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of Zn2+.
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Word Map
- 7.2.2.20
- enterica
-
zinc-regulated
-
calprotectin
-
zinc-responsive
-
zinc-limited
- salmonellosis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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+
=
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+
+
Zn2+-[zinc-binding protein][side 1]
=
+
+
+
[zinc-binding protein][side 1]
Synonyms
znuabc, high-affinity zinc transporter, high-affinity zinc uptake system, adcabc, zinc import system, high-affinity zinc incorporator, zn2+ uptake system, high-affinity zn2+ transporter, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adcABC
high-affinity zinc incorporator
high-affinity zinc transporter
high-affinity Zn2+ transporter
Pden1597
Zn2+ ABC transporter
Zn2+-specific transporter
Zn2+-transporting ATPase
-
-
-
-
ZnuA
znuABC
Zn2+ ABC transporter
-
-
-
-
znuABC
-
-
-
-
znuABC
-
composed of the periplasmic binding protein ZnuA, the ATPase ZnuC, and the integral membrane protein ZnuB
znuABC
-
gene name, znuA (formerly yebL) codes for the binding protein, znuC (formerly yebM) for the ATPase subunit, and znuB (formerly yebI) for the membrane component of the ABC transporter
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Zn2+-[zinc-binding protein][side 1] = ADP + phosphate + Zn2+[side 2] + [zinc-binding protein][side 1]
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, Zn2+-importing)
ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of Zn2+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mn2+-[manganese-binding protein][side1]
ADP + phosphate + Mn2+[side2] + [manganese-binding protein][side2]
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
ATP + H2O + Mn2+-[manganese-binding protein][side1]
ADP + phosphate + Mn2+[side2] + [manganese-binding protein][side2]
-
the enzyme binds Zn2+ with an affinity about 100fold greater than that for Mn2+
-
-
?
ATP + H2O + Mn2+-[manganese-binding protein][side1]
ADP + phosphate + Mn2+[side2] + [manganese-binding protein][side2]
-
the enzyme binds Zn2+ with an affinity about 100fold greater than that for Mn2+
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
the enzyme binds Zn2+ with an affinity about 100fold greater than that for Mn2+
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
the enzyme binds Zn2+ with an affinity about 100fold greater than that for Mn2+
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
Salmonella enterica ATCC 14028
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
Salmonella enterica MA6926
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
Salmonella enterica ATCC 14028
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
Salmonella enterica MA6926
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
ATP + H2O + Zn2+-[zinc-binding protein][side1]
ADP + phosphate + Zn2+[side2] + [zinc-binding protein][side2]
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
the high-affinity Zn2+ uptake is repressed by growth in the presence of 10 M Zn2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine Development.
Infections
Attenuated Salmonella enterica serovar Typhimurium lacking the ZnuABC transporter confers immune-based protection against challenge infections in mice.
Infections
Bile Salts Regulate Zinc Uptake and Capsule Synthesis in a Mastitis-Associated Extraintestinal Pathogenic Escherichia coli Strain.
Infections
The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice.
Infections
The ZnuABC operon is important for Yersinia ruckeri infections of rainbow trout, Oncorhynchus mykiss (Walbaum).
Infections
The ZupT transporter plays an important role in zinc homeostasis and contributes to Salmonella enterica virulence.
Neoplasms
Attenuated mutant strain of Salmonella Typhimurium lacking the ZnuABC transporter contrasts tumor growth promoting anti-cancer immune response.
Paratuberculosis
Identification and Characterization of Mycobacterium smegmatis and Mycobacterium avium subsp. paratuberculosis Zinc Transporters.
Plague
The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice.
Plague
Zinc transporters YbtX and ZnuABC are required for the virulence of Yersinia pestis in bubonic and pneumonic plague in mice.
Salmonella Infections
An attenuated Salmonella enterica serovar Typhimurium strain lacking the ZnuABC transporter induces protection in a mouse intestinal model of Salmonella infection.
Salmonella Infections
Attenuated Salmonella enterica serovar Typhimurium lacking the ZnuABC transporter: an efficacious orally-administered mucosal vaccine against salmonellosis in pigs.
Starvation
Identification and Characterization of Mycobacterium smegmatis and Mycobacterium avium subsp. paratuberculosis Zinc Transporters.
Starvation
Phenotypic profile linked to inhibition of the major Zn influx system in Salmonella enterica: proteomics and ionomics investigations.
Starvation
The ZupT transporter plays an important role in zinc homeostasis and contributes to Salmonella enterica virulence.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
a deletion mutant of subunit znuA drastically reduces the ability of Salmonella enterica to multiply in media deprived of zinc, impairs its ability to grow in Caco-2 epithelial cells, and lead to decreased ability to multiply in phagocytes under zinc starving conditions
malfunction
-
enzyme deletion mutants show lower resistance to oxidative stress under zinc deprivation compared to the wild type enzyme
malfunction
-
inactivation of the subunit gene znuA significantly decreases Escherichia coli O157:H7 ability to grow in zinc depleted media. Lack of subunit ZnuA affects the adhesion ability of the bacteria to cultured epithelial cells
malfunction
-
Salmonella strains producing a modified form of subunit ZnuA which lacks a characteristic histidine-rich domain exhibit a ZinT-dependent capability to import zinc either in vitro or in infected mice
malfunction
-
the absence of enzyme-mediated zinc uptake affects virulence-associated phenotypes of Escherichia coli CFT073 under zinc-depleted conditions. The subunit znuB-deletion mutant is significantly deficient in the formation of biofilm under static conditions and also shows a substantially reduced migration front of swarm cells
malfunction
Salmonella enterica MA6926
-
Salmonella strains producing a modified form of subunit ZnuA which lacks a characteristic histidine-rich domain exhibit a ZinT-dependent capability to import zinc either in vitro or in infected mice
-
malfunction
Salmonella enterica ATCC 14028
-
a deletion mutant of subunit znuA drastically reduces the ability of Salmonella enterica to multiply in media deprived of zinc, impairs its ability to grow in Caco-2 epithelial cells, and lead to decreased ability to multiply in phagocytes under zinc starving conditions
-
malfunction
-
the absence of enzyme-mediated zinc uptake affects virulence-associated phenotypes of Escherichia coli CFT073 under zinc-depleted conditions. The subunit znuB-deletion mutant is significantly deficient in the formation of biofilm under static conditions and also shows a substantially reduced migration front of swarm cells
-
physiological function
-
the enzyme contributes to the virulence of Escherichia coli CFT073 in the urinary tract
physiological function
-
the enzyme contributes to the virulence of Salmonella enterica, is required for Salmonella enterica growth in poor zinc environments, and contributes to Salmonella multiplication within eukaryotic cells and accumulates in intracellular environments
physiological function
-
the enzyme contributes to zinc acquisition and the development of lethal septicemic plague in mice
physiological function
-
the periplasmic proteins ZinT and ZnuA cooperate in the process of zinc recruitment as they form a stable binary complex in vitro. ZnuA is a protein involved in the frontline response to zinc deficiency, whereas ZinT participates in the bacterial response to more severe zinc deficiency
physiological function
-
the transporter plays a critical role in zinc uptake. The periplasmic protein ZinT contributes to the subunit ZnuA-mediated recruitment of zinc in the periplasmic space
physiological function
-
the wild type strain acquires Zn2+ by means of the enzyme to reduce intracellular reactive oxygen species levels and, so, prevent oxidative damage to cells
physiological function
Salmonella enterica MA6926
-
the periplasmic proteins ZinT and ZnuA cooperate in the process of zinc recruitment as they form a stable binary complex in vitro. ZnuA is a protein involved in the frontline response to zinc deficiency, whereas ZinT participates in the bacterial response to more severe zinc deficiency
-
physiological function
Salmonella enterica ATCC 14028
-
the enzyme contributes to the virulence of Salmonella enterica, is required for Salmonella enterica growth in poor zinc environments, and contributes to Salmonella multiplication within eukaryotic cells and accumulates in intracellular environments
-
physiological function
-
the enzyme contributes to the virulence of Escherichia coli CFT073 in the urinary tract
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ZNUC1_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
256
0
28441
Swiss-Prot
-
ZNUC1_HAHCH
Hahella chejuensis (strain KCTC 2396)
255
0
28178
Swiss-Prot
-
ZNUC2_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
243
0
26663
Swiss-Prot
-
ZNUC2_HAHCH
Hahella chejuensis (strain KCTC 2396)
244
0
26110
Swiss-Prot
-
ZNUC_ACIAD
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
259
0
29372
Swiss-Prot
-
ZNUC_AERHH
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049)
254
0
28323
Swiss-Prot
-
ZNUC_WOLTR
Wolbachia sp. subsp. Brugia malayi (strain TRS)
246
0
27139
Swiss-Prot
-
ZNUC_YERE8
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
252
0
27656
Swiss-Prot
-
ZNUC_YERPA
Yersinia pestis bv. Antiqua (strain Antiqua)
253
0
27620
Swiss-Prot
-
ZNUC_YERPN
Yersinia pestis bv. Antiqua (strain Nepal516)
253
0
27620
Swiss-Prot
-
ZNUC_YERPS
Yersinia pseudotuberculosis serotype I (strain IP32953)
253
0
27635
Swiss-Prot
-
ZNUC_ECOUT
Escherichia coli (strain UTI89 / UPEC)
251
0
27867
Swiss-Prot
-
ZNUC_EHRCR
Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
242
0
27901
Swiss-Prot
-
ZNUC_EHRRG
Ehrlichia ruminantium (strain Gardel)
242
0
27752
Swiss-Prot
-
ZNUC_EHRRW
Ehrlichia ruminantium (strain Welgevonden)
242
0
27752
Swiss-Prot
-
ZNUC_HAEDU
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
264
0
29297
Swiss-Prot
-
ZNUC_HAEI8
Haemophilus influenzae (strain 86-028NP)
268
0
29862
Swiss-Prot
-
ZNUC_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
268
0
29859
Swiss-Prot
-
ZNUC_HALHL
Halorhodospira halophila (strain DSM 244 / SL1)
260
0
27755
Swiss-Prot
-
ZNUC_HYDCU
Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2)
258
0
28732
Swiss-Prot
-
ZNUC_MAGMM
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
260
0
28329
Swiss-Prot
-
ZNUC_MAGSA
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
262
0
27554
Swiss-Prot
-
ZNUC_MANSM
Mannheimia succiniciproducens (strain MBEL55E)
264
0
29417
Swiss-Prot
-
ZNUC_MARN8
Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8)
257
0
28022
Swiss-Prot
-
ZNUC_PARDP
Paracoccus denitrificans (strain Pd 1222)
254
0
27209
Swiss-Prot
-
ZNUC_PECAS
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
252
0
27740
Swiss-Prot
-
ZNUC_RICTY
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
233
0
26300
Swiss-Prot
-
ZNUC_ROSDO
Roseobacter denitrificans (strain ATCC 33942 / OCh 114)
255
0
27038
Swiss-Prot
-
ZNUC_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
256
0
27296
Swiss-Prot
-
ZNUC_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
261
0
28545
Swiss-Prot
-
ZNUC_SALCH
Salmonella choleraesuis (strain SC-B67)
251
0
27685
Swiss-Prot
-
ZNUC_SALPA
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
251
0
27685
Swiss-Prot
-
ZNUC_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
251
0
27666
Swiss-Prot
-
ZNUC_SHIBS
Shigella boydii serotype 4 (strain Sb227)
251
0
27867
Swiss-Prot
-
ZNUC_SHIDS
Shigella dysenteriae serotype 1 (strain Sd197)
251
0
27882
Swiss-Prot
-
ZNUC_SHIF8
Shigella flexneri serotype 5b (strain 8401)
251
0
27814
Swiss-Prot
-
ZNUC_SODGM
Sodalis glossinidius (strain morsitans)
255
0
28413
Swiss-Prot
-
ZNUC_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
262
0
29100
Swiss-Prot
-
ZNUC_VIBPA
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
262
0
29012
Swiss-Prot
-
ZNUC_WIGBR
232
0
26396
Swiss-Prot
-
ZNUC_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
299
0
32084
Swiss-Prot
-
ZNUC_ALCBS
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
259
0
27718
Swiss-Prot
-
ZNUC_ALKEH
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
259
0
28016
Swiss-Prot
-
ZNUC_ANAMM
Anaplasma marginale (strain St. Maries)
245
0
27443
Swiss-Prot
-
ZNUC_ANAPZ
Anaplasma phagocytophilum (strain HZ)
243
0
27179
Swiss-Prot
-
ZNUC_BRUAB
Brucella abortus biovar 1 (strain 9-941)
298
0
32273
Swiss-Prot
-
ZNUC_BRUME
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
298
0
32334
Swiss-Prot
-
ZNUC_BRUSU
Brucella suis biovar 1 (strain 1330)
298
0
32247
Swiss-Prot
-
ZNUC_BUCAI
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
238
0
26814
Swiss-Prot
-
ZNUC_BUCAP
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
238
0
26998
Swiss-Prot
-
ZNUC_BUCBP
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
238
0
26842
Swiss-Prot
-
ZNUC_CERS4
Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)
243
0
26358
Swiss-Prot
-
ZNUC_CHRSD
Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)
240
0
26188
Swiss-Prot
-
ZNUC_ECOL5
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
251
0
27867
Swiss-Prot
-
ZNUC_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
251
0
27867
Swiss-Prot
-
ZNUC_PHOLL
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
257
0
28466
Swiss-Prot
-
ZNUC_PHOPR
Photobacterium profundum (strain SS9)
257
0
28428
Swiss-Prot
-
ZNUC_PSE14
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
265
0
28826
Swiss-Prot
-
ZNUC_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
269
0
29156
Swiss-Prot
-
ZNUC_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
269
0
29156
Swiss-Prot
-
ZNUC_PSEE4
Pseudomonas entomophila (strain L48)
257
0
27811
Swiss-Prot
-
ZNUC_PSEF5
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
261
0
28240
Swiss-Prot
-
ZNUC_PSEPF
Pseudomonas fluorescens (strain Pf0-1)
261
0
28242
Swiss-Prot
-
ZNUC_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
257
0
27741
Swiss-Prot
-
ZNUC_PSESM
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
264
0
28645
Swiss-Prot
-
ZNUC_PSEU2
Pseudomonas syringae pv. syringae (strain B728a)
262
0
28352
Swiss-Prot
-
ZNUC_PSYA2
Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4)
243
0
27387
Swiss-Prot
-
ZNUC_PSYCK
Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5)
243
0
27314
Swiss-Prot
-
ZNUC_RHIEC
Rhizobium etli (strain CFN 42 / ATCC 51251)
312
0
33857
Swiss-Prot
-
ZNUC_RHIL3
Rhizobium leguminosarum bv. viciae (strain 3841)
303
0
32818
Swiss-Prot
-
ZNUC_RICCN
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
233
0
26072
Swiss-Prot
-
ZNUC_RICFE
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
233
0
26117
Swiss-Prot
-
ZNUC_RICPR
Rickettsia prowazekii (strain Madrid E)
233
0
26205
Swiss-Prot
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
-
the Zn2+-bound protein is remarkably stable, maintaining its circular dichroism spectrum up to 90°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased under conditions of Zn2+ starvation
the enzyme gene cluster is derepressed by divalent metal ions such as Fe2+, Mn2+, Cu2+, and Cd2+
-
the enzyme transcription level is regulated by the Zn2+ concentration to maintain intracellular Zn2+ homeostasis
-
the expression of subunit znuA, regulated by Zur, is induced in zinc-poor media and in bacteria adhering to cultured epithelial cells
-
the expression of the enzyme is inducible when cells were grown in medium containing a metal chelator (EDTA), and this induction is specific for zinc depletion
the expression of the enzyme is reduced in response to increased zinc in a dose-dependent manner
enzyme expression is increased under conditions of Zn2+ starvation
-
enzyme expression is increased under conditions of Zn2+ starvation
-
-
the expression of the enzyme is inducible when cells were grown in medium containing a metal chelator (EDTA), and this induction is specific for zinc depletion
-
the expression of the enzyme is inducible when cells were grown in medium containing a metal chelator (EDTA), and this induction is specific for zinc depletion
-
-
the expression of the enzyme is reduced in response to increased zinc in a dose-dependent manner
-
the expression of the enzyme is reduced in response to increased zinc in a dose-dependent manner
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, T.; Yang, X.; Gao, F.; Zhao, C.; Kang, Y.; Wang, Y.; Shen, X.
Zinc acquisition via ZnuABC in Yersinia pseudotuberculosis facilitates resistance to oxidative stress
Ann. Microbiol.
66
1189-1197
2016
Yersinia pseudotuberculosis
-
brenda
Hantke, K.
Bacterial zinc transporters and regulators
Biometals
14
239-249
2001
Streptococcus pneumoniae, Escherichia coli, [Haemophilus] ducreyi
brenda
Gabbianelli, R.; Scotti, R.; Ammendola, S.; Petrarca, P.; Nicolini, L.; Battistoni, A.
Role of ZnuABC and ZinT in Escherichia coli O157 H7 zinc acquisition and interaction with epithelial cells
BMC Microbiol.
11
36
2011
Escherichia coli
brenda
Gunasekera, T.S.; Herre, A.H.; Crowder, M.W.
Absence of ZnuABC-mediated zinc uptake affects virulence-associated phenotypes of uropathogenic Escherichia coli CFT073 under Zn(II)-depleted conditions
FEMS Microbiol. Lett.
300
36-41
2009
Escherichia coli, Escherichia coli CFT073
brenda
Ammendola, S.; Pasquali, P.; Pistoia, C.; Petrucci, P.; Petrarca, P.; Rotilio, G.; Battistoni, A.
High-affinity Zn2+ uptake system ZnuABC is required for bacterial zinc homeostasis in intracellular environments and contributes to the virulence of Salmonella enterica
Infect. Immun.
75
5867-5876
2007
Salmonella enterica, Salmonella enterica ATCC 14028
brenda
Petrarca, P.; Ammendola, S.; Pasquali, P.; Battistoni, A.
The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage
J. Bacteriol.
192
1553-1564
2010
Salmonella enterica, Salmonella enterica MA6926
brenda
Ogura, M.
ZnuABC and ZosA zinc transporters are differently involved in competence development in Bacillus subtilis
J. Biochem.
150
615-625
2011
Bacillus subtilis, Bacillus subtilis 168
brenda
Patzer, S.I.; Hantke, K.
The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
J. Biol. Chem.
275
24321-24332
2000
Escherichia coli
brenda
Handali, M.; Neupane, D.; Roychowdhury, H.; Yukl, E.
Transcriptional regulation, metal binding properties and structure of Pden1597, an unusual zinc transport protein from Paracoccus denitrificans
J. Biol. Chem.
290
11878-11889
2015
Paracoccus denitrificans, Paracoccus denitrificans Pd1222
brenda
Bhubhanil, S.; Sittipo, P.; Chaoprasid, P.; Nookabkaew, S.; Sukchawalit, R.; Mongkolsuk, S.
Control of zinc homeostasis in Agrobacterium tumefaciens via zur and the zinc uptake genes znuABC and zinT
Microbiology
160
2452-2463
2014
Agrobacterium tumefaciens, Agrobacterium tumefaciens NTL4
brenda
Patzer, S.I.; Hantke, K.
The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
Mol. Microbiol.
28
1199-1210
1998
Escherichia coli
brenda
Bobrov, A.G.; Kirillina, O.; Fetherston, J.D.; Miller, M.C.; Burlison, J.A.; Perry, R.D.
The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice
Mol. Microbiol.
93
759-775
2014
Yersinia pestis
brenda
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