ID   E0WRV1_9ENTR            Unreviewed;       692 AA.
AC   E0WRV1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, 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};
GN   Name=prlC {ECO:0000313|EMBL:EFL92085.1};
GN   ORFNames=REG_0660 {ECO:0000313|EMBL:EFL92085.1};
OS   Candidatus Regiella insecticola LSR1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX   NCBI_TaxID=663321 {ECO:0000313|EMBL:EFL92085.1, ECO:0000313|Proteomes:UP000005726};
RN   [1] {ECO:0000313|EMBL:EFL92085.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSR1 {ECO:0000313|EMBL:EFL92085.1};
RX   PubMed=19840097;
RA   Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., Gibbs R.A.,
RA   Richards S., Moran N.A.;
RT   "Dynamics of genome evolution in facultative symbionts of aphids.";
RL   Environ. Microbiol. 0:0-0(2009).
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; GL379590; EFL92085.1; -; Genomic_DNA.
DR   RefSeq; WP_006704503.1; NZ_GL379590.1.
DR   AlphaFoldDB; E0WRV1; -.
DR   STRING; 663321.REG_0660; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   Proteomes; UP000005726; 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; 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:UP000005726};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          26..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   692 AA;  78596 MW;  EAB2EBF41480BA4A CRC64;
     MTNLSLTSPL PQFSAIHPEN IVSRVQAVLE ECRQAVDNIV AHPDPFVWDN LCQPLAELDN
     RLSCLWSPVS HLNAVKNNVA LREAYEQCLP LLSEFSTWLG QHKKLYQAYL SLQTGPTFSD
     LNAAQRKVVE NMLRDFKLSG IDLAPEQQER YGKIAARLSE LASTYSNNVL DATMGWSKLI
     TDINQLKGLP ESALAAAKMM AEAKQQEGWL FTLDMPSYLP VLTYADNSEL RKEMYSAFTT
     RASDQGPNAG KWDNNEIMEE MLGLRHELAQ LLGFASYADK SLATKMADNP QEVLRFLTDL
     AKRARPQAEK ELAQLRVFAK QQDDVSELAA WDITYYAEKQ KQYLFSINDE QLRPYFPVEG
     VLKGLFEVVK RIYGTDTKER QGVDVWHPDV RFFDLFDANG ALCGSFYLDL YARENKRNGA
     WMDSCVDSFR LSNGEWQKPV AYLTCNFNGP VGDTPALFTH DEVVTLFHEF GHGLHHMLTK
     IDISGVSGIN GVPWDAVELP SQFMENWCWE PQALAFISGH YQTQEPLPQE MLDKLLAVKN
     YHAGLFILRQ LELGLFDFRM HYEYDPVKGA QILPILNEVR KKVAITPAPT WGRFPHSFNH
     IFSGGYAAGY YSYLWAEVLS ADAFSRFKEE GIFNSVTGQS FLENILSLGG SEEPMILFKR
     FRGREPRLDA MLRDYGIQYD DVKNSAIQNN VI
//