ID A0A0C3RCG5_9PROT Unreviewed; 628 AA.
AC A0A0C3RCG5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KIO49055.1};
GN ORFNames=SQ11_08495 {ECO:0000313|EMBL:KIO49055.1};
OS Nitrosospira sp. NpAV.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=58133 {ECO:0000313|EMBL:KIO49055.1, ECO:0000313|Proteomes:UP000031969};
RN [1] {ECO:0000313|EMBL:KIO49055.1, ECO:0000313|Proteomes:UP000031969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NpAV {ECO:0000313|EMBL:KIO49055.1,
RC ECO:0000313|Proteomes:UP000031969};
RA Rice M.C., Lim C.K., Sayavedra-Soto L.A., Norton J.M., Klotz M.G.;
RT "Nitrosospira sp. NpAV genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, 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:KIO49055.1}.
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DR EMBL; JXQM01000012; KIO49055.1; -; Genomic_DNA.
DR RefSeq; WP_041513730.1; NZ_JXQM01000012.1.
DR AlphaFoldDB; A0A0C3RCG5; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000031969; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR017315; Pep_S8A_subtilisin_pbac-2.
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 PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF17957; Big_7; 2.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037901; Subtilisin_rel_Nmul_A1891; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 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|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 174..415
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 628 AA; 63970 MW; 925FECEA2A7A1214 CRC64;
MNIIKRALTA ADIEGPASGA VLLNIIPDSW LLSHALRRIV ALVLTGCMII PAVSDAAPPA
DAGPRSPGSE TWAKGRILVM PRAGLPEEEL AKILDAHGGK GRKIGQSDLY IVDLPGNASE
KAVAARLAHS PHFKFAELDY RESPEFVPND PYYGSAWHLP KIGANLAWDR SQGVGVTIAI
LDSGVDSAHP DLAPRMVPGW NFHDNNSNTS DVYGHGTQVA GAAAAAGNNG IGVTSVAVQT
KIMPIRVTDL SGSGYSSMIA NGLIYAADRG VRVANISFAN QPSRSVVVSA AQYMKSKGGL
VVVAAGNNGI NENFTPTTAM IPVSATDGSD MKTSWSSYGS YVAMAAPGTG IWTTSRGGGY
GAASGTSVSS PVAAGVVALI MAAKSTLLNT QVESLLYSTA VDLGAAGRDS YYGYGRVNAA
RAVQTAVGTT QTADTQAPAI SISAPLGGAT VTGLVGVNVV ATDNVGVTRV ELRVNSTTVA
IDTTAPFGFT WDSRGTPNGV ANLVAYAFDA AGNSKASAAV AVNVANGTVT VAKDTTPPVV
KIINPVAGNV SGNVVISLNA ADNSGAAGIT QMLYIDGVLK ATGSGSTLGY NWNTRPKSVA
AGTHTIRAVA KDKAGNASSA SVNVTVIR
//
