P58099 · C5AP_STRP1

Function

function

This virulence factor of S.pyogenes specifically cleaves the human serum chemotaxin C5a at '68-Lys-|-Asp-69' bond near its C-terminus, destroying its ability to serve as a chemoattractant.

Catalytic activity

  • The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59.
    EC:3.4.21.110 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

111811002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Active site130Charge relay system
Active site193Charge relay system
Active site512Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Cellular Componentmembrane
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    C5a peptidase
  • EC number
  • Alternative names
    • SCP

Gene names

    • Name
      scpA
    • Ordered locus names
      SPy_2010, M5005_Spy1715

Organism names

  • Taxonomic identifier
  • Strains
    • ATCC 700294 / SF370 / Serotype M1
    • ATCC BAA-947 / MGAS5005 / Serotype M1
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus

Accessions

  • Primary accession
    P58099
  • Secondary accessions
    • Q48WE2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue, propeptide.

TypeIDPosition(s)Description
Signal1-31
ChainPRO_000002715332-1147C5a peptidase
Modified residue1147Pentaglycyl murein peptidoglycan amidated threonine
PropeptidePRO_00000271541148-1181Removed by sortase

Post-translational modification

Cleaved by SpeB protease; leading to its degradation (PubMed:7730368).
Degradation by SpeB is probably strictly regulated to preserve integrity of C5a peptidase (Probable)

Keywords

Proteomic databases

Family & Domains

Features

Showing features for compositional bias, region, domain, repeat, motif.

TypeIDPosition(s)Description
Compositional bias33-65Polar residues
Region33-117Disordered
Compositional bias91-113Polar residues
Domain99-581Peptidase S8
Region1029-1150Disordered
Compositional bias1031-1107Basic and acidic residues
Repeat1034-10501
Region1034-11185 X 17 AA tandem repeats
Repeat1051-10672
Repeat1068-10843
Repeat1085-11014
Repeat1102-11185
Compositional bias1108-1123Polar residues
Motif1144-1148LPXTG sorting signal

Sequence similarities

Belongs to the peptidase S8 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,181
  • Mass (Da)
    129,487
  • Last updated
    2001-06-01 v1
  • Checksum
    3F9FC51763419CFC
MRKKQKLPFDKLAIALMSTSILLNAQSDIKANTVTEDTPATEQAVETPQPTAVSEEAPSSKETKTPQTPDDAEETIADDANDLAPQAPAKTADTPATSKATIRDLNDPSQVKTLQEKAGKGAGTVVAVIDAGFDKNHEAWRLTDKTKARYQSKEDLEKAKKEHGITYGEWVNDKVAYYHDYSKDGKTAVDQEHGTHVSGILSGNAPSETKEPYRLEGAMPEAQLLLMRVEIVNGLADYARNYAQAIIDAVNLGAKVINMSFGNAALAYANLPDETKKAFDYAKSKGVSIVTSAGNDSSFGGKTRLPLADHPDYGVVGTPAAADSTLTVASYSPDKQLTETATVKTADQQDKEMPVLSTNRFEPNKAYDYAYANRGMKEDDFKDVKGKIALIERGDIDFKDKIANAKKAGAVGVLIYDNQDKGFPIELPNVDQMPAAFISRKDGLLLKENPQKTITFNATPKVLPTASGTKLSRFSSWGLTADGNIKPDIAAPGQDILSSVANNKYAKLSGTSMSAPLVAGIMGLLQKQYETQYPDMTPSERLDLAKKVLMSSATALYDEDEKAYFSPRQQGAGAVDAKKASAATMYVTDKDNTSSKVHLNNVSDKFEVTVTVHNKSDKPQELYYQATVQTDKVDGKLFALAPKALYETSWQKITIPANSSKQVTIPIDVSQFSKDLLAPMKNGYFLEGFVRFKQDPTKEELMSIPYIGFRGDFGNLSALEKPIYDSKDGSSYYHEANSDAKDQLDGDGLQFYALKNNFTALTTESNPWTIIKAVKEGVENIEDIESSEITETIFAGTFAKQDDDSHYYIHRHANGKPYAAISPNGDGNRDYVQFQGTFLRNAKNLVAEVLDKEGNVVWTSEVTEQVVKNYNNDLASTLGSTRFEKTRWDGKDKDGKVVANGTYTYRVRYTPISSGAKEQHTDFDVIVDNTTPEVATSATFSTEDRRLTLASKPKTSQPVYRERIAYTYMDEDLPTTEYISPNEDGTFTLPEEAETMEGATVPLKMSDFTYVVEDMAGNITYTPVTKLLEGHSNKPEQDGSDQAPDKKPETKPEQDGSGQAPDKKPETKPEQDGSGQTPDKKPETKPEQDGSGQTPDKKPETKPEKDSSGQTPGKTPQKGQPSRTLEKRSSKRALATKASTKDQLPTTNDKDTNRLHLLKLVMTTFFLGLVAHIFKTKRTED

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias33-65Polar residues
Compositional bias91-113Polar residues
Compositional bias1031-1107Basic and acidic residues
Sequence conflict1072-1088in Ref. 2
Compositional bias1108-1123Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE004092
EMBL· GenBank· DDBJ
AAK34691.1
EMBL· GenBank· DDBJ
Genomic DNA
CP000017
EMBL· GenBank· DDBJ
AAZ52333.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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