ID   E6WWA5_PSEUU            Unreviewed;       676 AA.
AC   E6WWA5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   OrderedLocusNames=Psesu_2481 {ECO:0000313|EMBL:ADV28313.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV28313.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV28313.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) 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}.
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DR   EMBL; CP002446; ADV28313.1; -; Genomic_DNA.
DR   RefSeq; WP_013536140.1; NC_014924.1.
DR   AlphaFoldDB; E6WWA5; -.
DR   MEROPS; M03.004; -.
DR   KEGG; psu:Psesu_2481; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000008632; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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; IPR045666; OpdA_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          29..149
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          224..673
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   676 AA;  75531 MW;  D105B63791D6C1DE CRC64;
     MSPANPLLDF SGLPRFSEVR PEHIGPAIDA LLEQAEAAVE QAGTVSPVSW DSFVTPLEDA
     TERLWRAWGQ VSHLQAVVNT PELREAYNAN LPRVTRFGSS LGQNLALYSQ YKALAESPEY
     AGYDPVRRKV VDNALRDFRL GGAELDEASK QRFAAIQEEL AALSAKFSQN VLDATDAFAL
     YVEDESRLAG LPAEVVAAAR AAAEKDGRPG WKLTLQMPCY LPVQTYAEDR SLREALYRAH
     GLRASEAGPA ELDNSGNIDR IVALRGELAA LLGFSSYAEY SLATKMAQTP DEVLGFLRDL
     AGRALPFARR DRAELEAFAR DELCLDELQP WDLAWASEKL KQARYSYSEQ EVKQYFTEPK
     VLAGLFGVIE SLYQVKVKPD TAPLWHEDVR FYRVEDAQGR LLGQFYLDPY AREGKRGGAW
     MDDCRNRRLR ADGVQTPLVY VVCNFGKPVA GKPATLGFNE VTTLFHEMGH GLHQLLTAIG
     ELPVAGINGV EWDAVELPSQ FMENFCWEWE RVQAMTAHVD TGAPLPRELF DRMLAAKNFQ
     AGMFTVRQLE FALFDMELHS RFDPARDSVL QLLERVRDEV AVNRTPSWHR FPHQFSHIFA
     GGYAAGYYSY KWAEVLSADA YAAFEETPGQ LAETGARFLR EILSRGGSRS ALENFKAFRG
     REPSLDALLR HNGMAA
//