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Information on EC 3.4.22.B63 - sortase C

for references in articles please use BRENDA:EC3.4.22.B63
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B63 sortase C
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This record set is specific for:
UNIPROT: Q8E0S7
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
The enzyme from Bacillus anthracis cleaves the LPNT-/-A sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli [17074072]. The enzymes from Streptococcus pneumoniae and Enterococcus faecalis are required for efficient pilus assembly.
Synonyms
srtc1, srtc2, srtc-1, sortase c, srtc-2, srtc-3, srt-2, sortase c1, sortase c2, pilus-associated sortase c, more
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Dabcyl-ancillary protein 1-Edans + H2O
?
show the reaction diagram
preferred substrate of SrtC2
-
-
?
Dabcyl-ancillary protein 2-Edans + H2O
?
show the reaction diagram
preferred substrate of SrtC1
-
-
?
Dabcyl-BP-1 peptide-Edans + H2O
?
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Dabcyl-ancillary protein 1-Edans + H2O
?
show the reaction diagram
preferred substrate of SrtC2
-
-
?
Dabcyl-ancillary protein 2-Edans + H2O
?
show the reaction diagram
preferred substrate of SrtC1
-
-
?
Dabcyl-BP-1 peptide-Edans + H2O
?
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(trimethylammonium)ethyl thiol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00358 - 0.06036
Dabcyl-ancillary protein 1-Edans
-
0.01421 - 0.02733
Dabcyl-ancillary protein 2-Edans
-
0.02156 - 0.04385
Dabcyl-BP-1 peptide-Edans
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00104 - 0.0049
Dabcyl-ancillary protein 1-Edans
-
0.00041 - 0.00113
Dabcyl-ancillary protein 2-Edans
-
0.000731 - 0.00298
Dabcyl-BP-1 peptide-Edans
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.2 - 810
Dabcyl-ancillary protein 1-Edans
-
159 - 797
Dabcyl-ancillary protein 2-Edans
-
243 - 922
Dabcyl-BP-1 peptide-Edans
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptococcus agalactiae serogroup V ATCC BAA-611
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8E0S7_STRA5
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
305
0
34468
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoprotein, hanging drop vapor diffusion method, using 15-25% (w/v) polyethylene glycol 3350 and 0.2 M Tris buffer (pH 8.0-8.8) and 0.2 M ammonium acetate at 4°C. In complex with inhibitor 2-(trimethylammonium)ethyl thiol, hanging drop vapor diffusion method, using 1.6 M ammonium sulfate, 5% (w/v) polyethylene glycol 3350, and sodium cacodylate (pH 6.5) at 4°C
isofofm SrtC1, hanging drop vapor diffusion method, using 0.4 M sodium formate, 0.1 M Bis-Tris propane pH 6.5, and 22% (w/v) PEG 3350. Isoform SrtC1, hanging drop vapor diffusion method, using 0.26 M CaCl2, 19% (w/v) PEG 6000, 0.1 M HEPES pH 7.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F86A
the mutant shows decreased catalytic efficiency compared to the wild type
Y92A
the mutant shows increased catalytic efficiency compared to the wild type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography, and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3) cells
expressed in Escherichia coli Rosetta (DE3) pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Khare, B.; Fu, Z.Q.; Huang, I.H.; Ton-That, H.; Narayana, S.V.
The crystal structure analysis of group B Streptococcus sortase C1: a model for the "lid" movement upon substrate binding
J. Mol. Biol.
414
563-577
2011
Streptococcus agalactiae serogroup V (Q8E0S7), Streptococcus agalactiae serogroup V ATCC BAA-611 (Q8E0S7)
Manually annotated by BRENDA team
Cozzi, R.; Prigozhin, D.; Rosini, R.; Abate, F.; Bottomley, M.J.; Grandi, G.; Telford, J.L.; Rinaudo, C.D.; Maione, D.; Alber, T.
Structural basis for group B Streptococcus pilus 1 sortases C regulation and specificity
PLoS ONE
7
e49048
2012
Streptococcus agalactiae serogroup V (Q8E0S7), Streptococcus agalactiae serogroup V ATCC BAA-611 (Q8E0S7)
Manually annotated by BRENDA team