ID F9S1B1_9VIBR Unreviewed; 350 AA.
AC F9S1B1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative serine protease {ECO:0000313|EMBL:EGU41950.1};
GN ORFNames=VII00023_00035 {ECO:0000313|EMBL:EGU41950.1};
OS Vibrio ichthyoenteri ATCC 700023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU41950.1, ECO:0000313|Proteomes:UP000004605};
RN [1] {ECO:0000313|EMBL:EGU41950.1, ECO:0000313|Proteomes:UP000004605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU41950.1,
RC ECO:0000313|Proteomes:UP000004605};
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:EGU41950.1}.
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DR EMBL; AFWF01000104; EGU41950.1; -; Genomic_DNA.
DR RefSeq; WP_006711882.1; NZ_AFWF01000104.1.
DR AlphaFoldDB; F9S1B1; -.
DR MEROPS; S01.515; -.
DR OrthoDB; 9813836at2; -.
DR Proteomes; UP000004605; 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:SF99; AQUARIUS-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, ECO:0000313|EMBL:EGU41950.1};
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..350
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003386449"
FT DOMAIN 25..276
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 350 AA; 37625 MW; 380211AD81B32E28 CRC64;
MQKLMLIGAI ALSSSAHSIE VSPFIINGSP VVIDNYPSFT SLFYENLVGG YTTSFCGATA
LNSDYVLTAA HCIVGNSRLE QVTVALQLVN ETNYVPGAPL RVSDFFVPAT YIESSSRLWP
DDIAILKLET SLPTGDHLDK LNFSVFGDLP AADTYVTIGH GLVYNSGTGR YQNDNELLET
TLTPLPLSQC KAHFGSNFTD KQICFDGTLP DTELQNSPCD GDSGGPVYRL TGSGYIQVGI
TSFGLEQCGD PTISTQVTSA FTNVAHYEDW IRNVLDGNVV STYRVVEQDG ERVVIDNSST
ASSGANSESG GSSGGSVSVI SLLGLLFISY MRQCSRMRIS ELSNRPRSQN
//
