ID A4C865_9GAMM Unreviewed; 679 AA.
AC A4C865;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=PTD2_07049 {ECO:0000313|EMBL:EAR28780.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR28780.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR28780.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR28780.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC Ala commonly occur as P1 or P1' residues, but more distant residues
CC are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC Evidence={ECO:0000256|ARBA:ARBA00024603};
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|ARBA:ARBA00006040, 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:EAR28780.1}.
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DR EMBL; AAOH01000003; EAR28780.1; -; Genomic_DNA.
DR RefSeq; WP_009838042.1; NZ_AAOH01000003.1.
DR AlphaFoldDB; A4C865; -.
DR STRING; 87626.PTD2_07049; -.
DR MEROPS; M03.004; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_1_6; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000006201; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF19310; TOP_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 30..147
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 221..676
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 679 AA; 76760 MW; C97E4F877D046657 CRC64;
MTNPLINLEG LPPFSQIKPE HIVPALKQGI EKCRKTIDEV LTHPTPTWQN FIAPLEEVDD
ELSRLWSPVS HMHSVVNSPE LREQYDVCLP LISEYSTFVG QHQGLYQGYQ AIFDSPEFAS
LSVAQQKVIT NALRDFKLSG ISLSPEKQQR YGEISARLSE LAAKYGNNVM DATQAWQKHI
TDEAQLSGLP ESAKALAAQT AQSKNLEGWL FTLDFPSYLP VMTYADSQEL RHETYVAFAT
RASEQGPNAG EFDNSAIMNE QLALRHELAQ LLDFENYAEH SLATKMAENT AQVFDFLNDL
AARSKPQAQQ ELAEVVEFAK QTHGVDKLEA WDIGYYSEKL KQQKYAISDE VLRPYFPANR
VLSGLFETVK RLFGITVVEV NGIDTWHPDV RFFDIIDEYN NKRGSFYLDL YARDNKRGGA
WMDDCIGRKV RQNGELQLPV AYLVCNFNKA VGNKPALFTH NEVTTLFHEF GHGLHHMLTK
IEAGAVSGIN GVAWDAVELP SQFLENWCYE EEALAFISGH YETHEPLPKE LLDKLLAAKN
YQSAMMMVRQ IEFSLFDFHI HADFKVDAKE HIQATIDAVR ERVAVIKAPH FNRFQHGFSH
IFAGGYSAGY YSYKWAEVLS ADAFSRFEEE GVFNTQTGRS FMNNILEMGG SLEPMELFTA
FRGRAPQIDA LLRHSGIGA
//
