KEGG ENZYME: 3.4.21.110

ENZYME: 3.4.21.110

Entry

EC 3.4.21.110               Enzyme

Name

C5a peptidase;
streptococcal C5a peptidase;
ScpA;
ScpB;
SCPA

Class

Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases

Reaction(IUBMB)

The primary cleavage site is at His67!Lys68 in human C5a with a minor secondary cleavage site at Ala58!Ser59

Comment

This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate specificity. Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a. Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties [1,4]. Belongs in peptidase family S8A.

History

EC 3.4.21.110 created 2006

Orthology

K08652

C5a peptidase

Genes

LAO:	AOX59_17515

SPY:	SPy_2010(scpA)

SPZ:	M5005_Spy1715(scpA)

SPYM:

M1GAS476_1768(scpA)

SPYA:

A20_1761c(scpA)

SPM:	spyM18_2074(scpA)

SPG:	SpyM3_1726(scpA)

SPS:

SPs1724

SPH:	MGAS10270_Spy1782(scpA)

SPI:	MGAS10750_Spy1807(scpA)

SPJ:	MGAS2096_Spy1744(scpA)

SPK:	MGAS9429_Spy1720(scpA)

SPF:	SpyM51681(scpA)

SPA:	M6_Spy1718

SPB:	M28_Spy1700(scpA)

STG:	MGAS15252_1558(scpA)

STX:	MGAS1882_1619(scpA)

SOZ:	Spy49_1669c(scpA)

STZ:	SPYALAB49_001698

SPYH:

L897_08565

SAG:

SAG0416

SAN:	gbs0451 scpB

SAK:	SAK_1320(scpB)

SAGS:

SaSA20_0382

SAGL:

GBS222_0377

SAGM:

BSA_13140 BSA_5040

SAGI:

MSA_4990

SAGR:

SAIL_5100

SAGP:

V193_02285

SAGC:

DN94_02285

SAGT:

GBSCOH1_0396 GBSCOH1_1144

SAGE:

EN72_02485 EN72_06820

SAGG:

EN73_02430 EN73_06360

SAGN:

W903_0519(scpA)

SAGJ:

ID870_07205

SEZ:	Sez_0946(scpZ)

SEQ:

SZO_10150

SEZO:

SeseC_01242(vpr)

SEQU:

Q426_04435

SUB:	SUB1154(scpA)

SDS:	SDEG_0933(scpB)

SDA:	GGS_0906(scpB)

SDC:	SDSE_0972(scpA)

SDQ:	SDSE167_1040(scpB)

SIK:

K710_0995

SIQ:	DQ08_04525

SIO:	DW64_04520

SMEN:

SAMEA4412692_1954(scpA_2)

SCAI:

NCTC12191_00740(scpA_4)

SPSU:

NCTC13786_00254(scpA_1)

SPOC:

NCTC10925_00915(scpA_1)

LPAR:

FAM21731_01264

LHIL:

G8J22_01096

CLO:	HMPREF0868_0979

VCOP:

MM50RIKEN_19220

ANR:	Ana3638_10365

TSF:	NQ543_11830

» show all

Reference

1 [PMID:3906656]

Authors

Wexler DE, Chenoweth DE, Cleary PP.

Title

Mechanism of action of the group A streptococcal C5a inactivator.

Journal

Proc Natl Acad Sci U S A 82:8144-8 (1985)
DOI:10.1073/pnas.82.23.8144

Reference

2 [PMID:1996961]

Authors

Bohnsack JF, Mollison KW, Buko AM, Ashworth JC, Hill HR.

Title

Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus.

Journal

Biochem J 273 ( Pt 3):635-40 (1991)
DOI:10.1042/bj2730635

Reference

3 [PMID:1452354]

Authors

Cleary PP, Prahbu U, Dale JB, Wexler DE, Handley J.

Title

Streptococcal C5a peptidase is a highly specific endopeptidase.

Journal

Infect Immun 60:5219-23 (1992)
DOI:10.1128/IAI.60.12.5219-5223.1992

Reference

4 [PMID:12354115]

Authors

Anderson ET, Wetherell MG, Winter LA, Olmsted SB, Cleary PP, Matsuka YV.

Title

Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes.

Journal

Eur J Biochem 269:4839-51 (2002)
DOI:10.1046/j.1432-1033.2002.03183.x

Reference

5 [PMID:10809707]

Authors

Stafslien DK, Cleary PP.

Title

Characterization of the streptococcal C5a peptidase using a C5a-green fluorescent protein fusion protein substrate.

Journal

J Bacteriol 182:3254-8 (2000)
DOI:10.1128/JB.182.11.3254-3258.2000

Reference

6 [PMID:16565520]

Authors

Terao Y, Yamaguchi M, Hamada S, Kawabata S.

Title

Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils.

Journal

J Biol Chem 281:14215-23 (2006)
DOI:10.1074/jbc.M513408200

Other DBs

ExplorEnz - The Enzyme Database:

3.4.21.110

IUBMB Enzyme Nomenclature:

3.4.21.110

ExPASy - ENZYME nomenclature database:

3.4.21.110

BRENDA, the Enzyme Database:

3.4.21.110

CAS:	100179-39-3

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Gene (65)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (62)   
   KEGG MGENES (2)   
Protein sequence (4337)   
   UniProt (3604)   
   SWISS-PROT (6)   
   RefSeq(pep) (722)   
   PDBSTR (5)   
DNA sequence (3953)   
   RefSeq(nuc) (3402)   
   GenBank (281)   
   EMBL (270)   
3D Structure (4)   
   PDB (4)   
Protein domain (13)   
   InterPro (13)   
All databases (8372)   

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