ID C9QH96_VIBOR Unreviewed; 327 AA.
AC C9QH96;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Elastase 2 {ECO:0000313|EMBL:EGU51183.1};
GN ORFNames=VIOR3934_00900 {ECO:0000313|EMBL:EGU51183.1};
OS Vibrio orientalis CIP 102891 = ATCC 33934.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU51183.1, ECO:0000313|Proteomes:UP000002817};
RN [1] {ECO:0000313|EMBL:EGU51183.1, ECO:0000313|Proteomes:UP000002817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102891 / ATCC 33934 {ECO:0000313|Proteomes:UP000002817};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:EGU51183.1}.
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DR EMBL; AFWH01000019; EGU51183.1; -; Genomic_DNA.
DR RefSeq; WP_004411313.1; NZ_AFWH01000019.1.
DR AlphaFoldDB; C9QH96; -.
DR STRING; 675816.VIA_000801; -.
DR MEROPS; S01.515; -.
DR PATRIC; fig|675816.5.peg.1725; -.
DR eggNOG; COG5640; Bacteria.
DR OrthoDB; 9813836at2; -.
DR Proteomes; UP000002817; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..327
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003000553"
FT DOMAIN 25..271
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 327 AA; 35381 MW; 46BA35EB780C3F8D CRC64;
MRSISVLASS LLAFSAHSAE VTPYIVNGTD ISASSYPDFV SLFYDRINYD GLYGKGPYCG
GTLLDEQHVL TAAHCIYGDS NYQLFTSVVP QLQNESDFPN SVQQRVMVNE YYYPSTYNDS
TLYDDIAIVK LASPITAVNT YVALADDSER GTYRQTSEDF YAVGHGNTES NYDSTKELQR
TKLKWVDNTT CDANYTTDAS ENLCMDGAAT VTYDNATCQG DSGGPLYWNG KQVGITSFGP
QTCGNPAVTA NSVFTEVALT KHKDWINSVL SGNEAPIVTV TDAQRNTALG ITTPTDSGGG
GGSLGIFVLS ALGLLGWRRR LNSSNFK
//
