ID A0A1B1EAL6_VIBNA Unreviewed; 540 AA.
AC A0A1B1EAL6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ANQ25788.1};
GN ORFNames=BA894_04710 {ECO:0000313|EMBL:ANQ25788.1};
OS Vibrio natriegens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ25788.1, ECO:0000313|Proteomes:UP000092577};
RN [1] {ECO:0000313|EMBL:ANQ25788.1, ECO:0000313|Proteomes:UP000092577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ25788.1,
RC ECO:0000313|Proteomes:UP000092577};
RA Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT "Developing Vibrio natriegens as a novel, fast-growing host for
RT biotechnology.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP016351; ANQ25788.1; -; Genomic_DNA.
DR RefSeq; WP_065296503.1; NZ_CP016351.1.
DR AlphaFoldDB; A0A1B1EAL6; -.
DR STRING; 691.BA893_04455; -.
DR OrthoDB; 9813836at2; -.
DR Proteomes; UP000092577; Chromosome 1.
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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR013783; Ig-like_fold.
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; PTHR24264:SF65; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24264; TRYPSIN-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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008521764"
FT DOMAIN 36..273
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 540 AA; 58386 MW; 710D8D64F653812D CRC64;
MKKTLVAFLI GMTLPATTMA DTDTLNPFQN DVSTRIIGGE PANTTDWRFI ASIVHKDQPA
YLGHFCGGSF LGGKYVLTAA HCVADTNADD IDIVLGLYDQ TNESQAQRIA VQNIYTHHAY
NSYTTNNDIA LIELAHSVDS ATIDLATPTV LDSVQAGDKL HVAGWGNTST TGTVFPTVLQ
QVDLEYVDRA TCQNLEGNYS NVSDDGICAG YISGGKDSCQ GDSGGPLIVD DNGINKLLGV
VSWGEGCAKP EAYGVYANVA HFQQNGWIDS HRNTISYTQY RDLRLVERKA QQETFTIRND
EADSPLNITD ITLSSGLTIA EDTCIETLSP SESCQITVGY YPTYAASIDT IEVTTDHPKL
PKLSTTFEYM GVDKASNSLS SAIPLTGVNV YTNNYAWTAE NGELHSADMG AATGESILYL
TDLPKGKLTM DLKVLSDGFD YFVVYINGQM YDYTNQLLDY TEVSADLYRT SNTVMLAYVK
NYAETGGFDA HANIRNIKMA ASADNDGDNS VKSKSSSGGS LSIGLLMLLA AGSFLRRKRG
//
