ID A8T1J7_9VIBR Unreviewed; 599 AA.
AC A8T1J7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative oligopeptidase {ECO:0000313|EMBL:EDP60172.1};
GN ORFNames=AND4_02148 {ECO:0000313|EMBL:EDP60172.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP60172.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP60172.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP60172.1,
RC ECO:0000313|Proteomes:UP000005159};
RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA Milton D.L., Gonzalez J.M., Pinhassi J.;
RT "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT starvation.";
RL PLoS Biol. 8:E1000358-E1000358(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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:EDP60172.1}.
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DR EMBL; ABGR01000002; EDP60172.1; -; Genomic_DNA.
DR RefSeq; WP_009841710.1; NZ_ABGR01000002.1.
DR AlphaFoldDB; A8T1J7; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000005159; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR034006; M3B_PepF_2.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 106..174
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 249..581
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 599 AA; 67454 MW; FD5BD1E0BB0AE14C CRC64;
MTAPSWDLSI VYNDLADFRI QDDIALVEQC IDLLNKQSAD CNSVEVMQNA ILTSEAASRL
AGTIANFANC YASVDATNTE AKALLGRMTR IFSELSQAYS AFELKLTHAD EEFITRVLDH
ENPDICGQAF SILNSRKLAD TRLSTEEEKL LAAMSVDGKS AWGKLYNNLT GSLKVKLDYA
DGKSEALGFS QAASLLYGSE FERQEAAWRG VQKAMATHQE SFASILNALS GWRLTENKKR
STKCDVHFLD PSLHGSRIRA ETLDAMMKVA KDSREIGQKA GLLMAKVHGL DEMKPWNHLA
AMPALSGEAK VYPFDEAIDV ICEAFETVSP DMSEFVRMMV QNGWIDAAPN ANKRLGAYCT
KLPATRTPLV FMTWSGSRSD LMTLAHELGH AFHNWVIRDL PLCQTYYPMT LAETASIFAE
NIVRDHLISK AESVDDKLEM LWEELSSALA LMINIPVRYE FEKAFYERRQ EGELTADELC
ELMSATWKGW YGDVMSEADP YFWASKLHFS ISSVSFYNYP YLFGFLFSKG IYAQRDAKGD
RFYGDYVDLL RDTGNMMAEE VVAKHLSMDL TQAEFWQQSV ELVRVKVDEF ERLLAQRGE
//
