ID   J3Z4K4_9ENTR            Unreviewed;       683 AA.
AC   J3Z4K4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
DE   Flags: Precursor;
GN   ORFNames=A359_08630 {ECO:0000313|EMBL:AFP85229.1};
OS   secondary endosymbiont of Ctenarytaina eucalypti.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=1199245 {ECO:0000313|EMBL:AFP85229.1, ECO:0000313|Proteomes:UP000003936};
RN   [1] {ECO:0000313|EMBL:AFP85229.1, ECO:0000313|Proteomes:UP000003936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ceuc_S {ECO:0000313|EMBL:AFP85229.1};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
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; CP003546; AFP85229.1; -; Genomic_DNA.
DR   RefSeq; WP_014888526.1; NC_018419.1.
DR   AlphaFoldDB; J3Z4K4; -.
DR   MEROPS; M03.004; -.
DR   KEGG; sect:A359_08630; -.
DR   PATRIC; fig|1199245.3.peg.992; -.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000003936; Chromosome.
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; 1.10.1370.40; -; 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:UP000003936};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          28..149
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          222..677
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   683 AA;  77418 MW;  C4475993C767A48A CRC64;
     MTNPLLTSFL LPPFTTICPE CIVPAVKAAI EQCRHTVEEV VAQSEPFTWE NLCYPIADAD
     DRLSRIWSPV SHLNAVKNSE ELRIAYDQSL TLLSAYSTWV GQHAGLYQAY RKLRAGKYYA
     QLTLAKKKVV DNTLRDFELS GIGLSEEKQK RFGDILACLA KLGSAYSNNV MDATMGWSKL
     ITDAGLLTSM PDSAIAAAYE KAKARGKTGW LLTLDTPSYL LVLTYCNSAI LREEIYRAYN
     TRASDQGPDA GKWDNGPLMS EILELRHEQA ILLGFESYAD QSLATKMAKN PQRVLNFLTD
     LAERGRNRGE QELMQLCDFA HLHFGCDKIN PWDIAYYSEK QKQHLFSIND QMLRPYFPES
     RVLKGLFKVV KRIYDITVKE LENVETWHPD VRFFGLFDKN DELCGSFYLD LYVRENKRSG
     AWMDNCVSMM RKADGTLQKP VAYLTCNFNC PISGKPALFT HNEVITLFHE LGHGLHHILT
     CIDVPGVAGI SGVPWDAVEL PSQFMENYCW QSEALALISG HYETGKPLST EILNKLIAAK
     HYQAALLILK QLEFGLFDFR IHYEYKPEHG ARILEILTEV KKQVSVLPAL VWGRFPHTFS
     HIFSGGYAAG YYSYLWAEVL SADIWSRFEE EGIFNQETGQ LFLDTILSRG GSEDPMVLFT
     RFRGREPQLD AMLQHYGIQV SGT
//