ID V6ARF8_9ARCH Unreviewed; 680 AA.
AC V6ARF8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=NITUZ_140307 {ECO:0000313|EMBL:CDI05232.1};
OS Candidatus Nitrosotenuis uzonensis.
OC Archaea; Nitrososphaerota; Nitrosotenuis.
OX NCBI_TaxID=1407055 {ECO:0000313|EMBL:CDI05232.1, ECO:0000313|Proteomes:UP000018159};
RN [1] {ECO:0000313|EMBL:CDI05232.1, ECO:0000313|Proteomes:UP000018159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N4 {ECO:0000313|EMBL:CDI05232.1,
RC ECO:0000313|Proteomes:UP000018159};
RX DOI=10.1371/journal.pone.0080835;
RA Lebedeva E.V., Hatzenpichler R., Pelletier E., Schuster N., Hauzmayer S.,
RA Bulaev A., Grigor'eva N.V., Galushko A., Schmid M., Palatinszky M.,
RA Le Paslier D., Daims H., Wagner M.;
RT "Enrichment and Genome Sequence of the Group I.1a Ammonia-Oxidizing
RT Archaeon ?Ca. Nitrosotenuis uzonensis? Representing a Clade Globally.";
RL PLoS ONE 0:0-0(2013).
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|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:CDI05232.1}.
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DR EMBL; CBTY010000006; CDI05232.1; -; Genomic_DNA.
DR AlphaFoldDB; V6ARF8; -.
DR STRING; 1407055.NITUZ_140307; -.
DR Proteomes; UP000018159; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034213; S8_Vpr-like.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003355};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003355};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU003355}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 660..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..443
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 247..341
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 63
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1"
SQ SEQUENCE 680 AA; 73275 MW; 67A063048A39B2F8 CRC64;
MKNPSVVVFC FCLIASCIIL LSNKIHDEPA LDIQLDKSSK YVGVQQPHGL GFTGNGIKVA
VIDTGVDYNH PDLLGFGHDS KVVGGYDFVE NDNSPMDING HGTEVAGIIA ANGIMRGIAP
DAKILAYRVS DTGNAVSSEL IVNAIKRAIS DGADIINISL GVNRTNDRIE DAINDAVRSG
VVVIVAAGNS GPDRMTIGSP GKDPHAITVG ATYNNITASL VATLQVDGKR FQVLPMVGMQ
PTSQTITGEI VFGKYGREED LAKIDAKDKI LLVQRGSDKE NELIYFSQKE KNSANAGAKA
LIVFNNEPGI FLGDLRNKEE GPDYKPRIPT VSISNEDGLD LANMLQNKTV GTINIFYHPD
FVSFFSSRGP VSPFYIKPNL VAPGVFVNTT SINGGYNLTS GTSFAAPHVA GASALLLQKS
PSLSPQEVAS ILTTTADPVA DTFGTGFPYE VSGAGRLNVT RAFGANLIII PDHAIFDLSP
FETSSTTIFQ LKTLNQEDSD IQVEFDFEHP VAEFSYSISG NLLEITASLV DQSAGQYEGR
IIISDGQTKY RIPVILRISD AAIHVSDDGG KLDFSLYYQE EWSYAKISVF NSDSRLVNSV
SVTPTRHEPV AIYQPGTYWI QAELKANNET KTVYSSIIVE HATQRQMFDL RALNIPGQQV
LIVVLAVSGI IALGLIIRLR
//
