ID F3UFC7_STRSA Unreviewed; 1506 AA.
AC F3UFC7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=C5a peptidase {ECO:0000256|ARBA:ARBA00020956};
DE EC=3.4.21.110 {ECO:0000256|ARBA:ARBA00012942};
DE AltName: Full=SCP {ECO:0000256|ARBA:ARBA00030432};
GN Name=prtS {ECO:0000313|EMBL:EGJ35857.1};
GN ORFNames=HMPREF9393_2331 {ECO:0000313|EMBL:EGJ35857.1};
OS Streptococcus sanguinis SK1056.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888820 {ECO:0000313|EMBL:EGJ35857.1, ECO:0000313|Proteomes:UP000004171};
RN [1] {ECO:0000313|EMBL:EGJ35857.1, ECO:0000313|Proteomes:UP000004171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1056 {ECO:0000313|EMBL:EGJ35857.1,
RC ECO:0000313|Proteomes:UP000004171};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This virulence factor of S.pyogenes specifically cleaves the
CC human serum chemotaxin C5a at '68-Lys-|-Asp-69' bond near its C-
CC terminus, destroying its ability to serve as a chemoattractant.
CC {ECO:0000256|ARBA:ARBA00002909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The primary cleavage site is at 67-His-|-Lys-68 in human C5a
CC with a minor secondary cleavage site at 58-Ala-|-Ser-59.;
CC EC=3.4.21.110; Evidence={ECO:0000256|ARBA:ARBA00001404};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGJ35857.1}.
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DR EMBL; AFFL01000010; EGJ35857.1; -; Genomic_DNA.
DR RefSeq; WP_002923350.1; NZ_GL890990.1.
DR PATRIC; fig|888820.3.peg.2277; -.
DR HOGENOM; CLU_001768_4_0_9; -.
DR Proteomes; UP000004171; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.120.1850; Ebh helix bundles repeating unit (S and A modules); 2.
DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR009063; Ig/albumin-bd_sf.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF07554; FIVAR; 3.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF46997; Bacterial immunoglobulin/albumin-binding domains; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1506
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003301815"
FT DOMAIN 3..26
FT /note="YSIRK Gram-positive signal peptide"
FT /evidence="ECO:0000259|Pfam:PF04650"
FT DOMAIN 194..658
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 458..532
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 681..791
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 30..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 597
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1506 AA; 163219 MW; 0ED5F5CB8B3B8693 CRC64;
MQRQRFSLRK YKFGLASVLL GTALVFGAGQ ARADEQATAS SSGQGQPTAA VVSATEPASQ
SARLESQPAA QAPVEKAAPA SFESAASSTE QASQPSTTEA KEAAAAPVEK GATSSSEEAS
SSAEKVTQPS ATQTKPTDPA SPTAESPSAA NSEKPAANPD AVAESPTSRD AKPSSISTNE
IIKVPQTWSQ GYKGQGRVVA IIDSGLDVHH EVLKISDPSK AKYQTEAALE EAKKKAGIDY
GKWYNNKVVY AYNYIDGDDN VKEKNSYSHG MHVTGITAGN PNKKAPNDEY VYGVAPEAQV
MFMRVFSDRQ RTTSDAIYIK AIDDAVALGA DTINMSLGSA TGSTVDVSPS LQAAIERARA
KGVSVIIAAG NDNTFGSEYS KPLVENPDYG LVSSPSTAES SISVASVNNT VLTEEVMEVR
GLEKNDKLLN GHFSYSMGET NATFEKGKEY EYVHVGLGRE EDFAGKDLTG KLALIQRGSF
TFAEKVRNAI SHGAVGALIY NNVDGANLTM SLDSESKKVP SAFISKEYGE ALAAGNYKVV
FNGLKVNRPH PGASSLSDFS SWGVTTDGLL KPDVTAPGGD IYSSLNDNTY GSMKGTSMAT
PHVAGVAALV KEYLLQHYPE LTPAQNADLV KALLMSTAKL HVNKETGVYT SPRQQGAGIV
DTAAAISTGL YVTGDNQYPS VSLGNVQDSF TFDVTVHNIT DKDRTLKMIV NTNTDAVKDG
YFTLTPRKLT ETVWPEVTVK AHSSQKVTVK VNTAKFAEEL IKQMPNGYFL EGFVRFVDPA
DDGDVVSLPF MGFRGEFQDL PAVERPIYNL VQEGKSGFYY PVPEDKSILS DDNVSSLVTE
SNDKLYSTGR TAARSSIVLG TAENADGKHV LQLGADGKIR LAFSPNGDGN QDSIQYRTVL
YRNVNNLTAS VYTADDKDYR FPIWQSSTIR EGRKNYYSGQ SDNPKSYLLE DTYWDGRDSK
GEKLEDGFYT YVVRYTPDVP GAKEQQISFN LQIDNQKPLI SSGYISTKDG AETFTARKPK
DVGNGGILRE QVFYLQADEK GKETYKAVDD FGIERDYERR VYISANADGS YTLPKGVDKS
KIFYVVEDYA GNRDSIALSE LVSAENDGRI RVALVDANTH QDVSSTFVYR IKDSKGKYVE
LDKGKKINAL PFGRYTAEIF TYDKDELRFY SALTQEFELT AQDSFKTIEF LVKKLVFAPV
SVAFDQAVPK NTQVVLKNNN GDAYTLPAEL FGKHAFGRSV AAGFYSVFVN LPTGYELWES
EPTVEVKEGK NNLLKLGVIV KSGLLAAVNQ QSSLVGTAQY YNASAAKRTA YDQAYQAAKE
ALTSKLTQAQ VDDVRAKLET ASADLDGKDS DIAAVKAAVE AYAATTKTGA YANAKDRTRR
AYDKAFQAVA LLLVQDKVTQ EQIDTALAQL TTAEKKLDGK ATNFTNLKKL VDDEVHYQAI
SNKFIYATDA VKAAYLEAYA QAKEVLTNPG ASQEDVKEAI ANLRAAKRKL DGRKPRVVRP
KKPKQV
//
