ID   L0E2C8_THIND            Unreviewed;       685 AA.
AC   L0E2C8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   Name=prlC [H] {ECO:0000313|EMBL:AGA35443.1};
GN   OrderedLocusNames=TVNIR_3819 {ECO:0000313|EMBL:AGA35443.1};
OS   Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA35443.1, ECO:0000313|Proteomes:UP000010809};
RN   [1] {ECO:0000313|Proteomes:UP000010809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC   {ECO:0000313|Proteomes:UP000010809};
RA   Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA   Ravin N.V., Popov V.O.;
RT   "Complete sequence of Thioalkalivibrio nitratireducens.";
RL   Submitted (DEC-2012) 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; CP003989; AGA35443.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0E2C8; -.
DR   STRING; 1255043.TVNIR_3819; -.
DR   MEROPS; M03.004; -.
DR   KEGG; tni:TVNIR_3819; -.
DR   PATRIC; fig|1255043.3.peg.3854; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   Proteomes; UP000010809; 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; 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; 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          31..153
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          228..681
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   685 AA;  77464 MW;  6C9088C6AEA1713C CRC64;
     MGAAVSNPLL ATENLPAFRS IRPEHVEPAV ERVLAENRAA LADLLSALPE RPGWNDFVVP
     LEQLENRLDA VWSPVRHLNS VMNSDALRAA YNACLPKLSE YASELSQNAE LYAAFDRLAR
     SPGFENESPD RQKLVRDALR DFHLSGVDLP EDRKARLRKI DARLSALTAR FEENVLDATQ
     SWTLHLPDAG RLAGVPDSSR AMLAQNARER DLDGYVITLD FPSYHAILTY ADDRDLREQV
     YTAYATRASD QGPDAGRYDN SEVMLEILRL REEKARITGF PHHAERSLAT KMADRPETVE
     RFLQDLAVRA RPYAEADLAE MREYAATRLG LTELQSWDYG YIAEKIRADR LGLSQEMLKP
     YFPADRVVAG LFGLVERLFG VSITEDPSVE TWHDDVRYFV IRDRAGAERA GFYFDLYARS
     AKRGGAWMDV CRSRFVHGSV HQLPVAYMTC NSTPPVDGKP ALFTHDEVIT LFHEFGHGLH
     HMLTRVDHPE IGGINGVEWD AVELPSQFME NWCWEREALD LFARHHETGE PMPDDLFERM
     LGTRHFQSAL QLLRQVEFAL FDMRLHSGPA PEATNDVQQL LDRVREEVAV VRPPSFNRFQ
     HGFAHIFAGG YAAGYYSYKW AEVLSADAFA RFEEEGLFSQ EVGSAYLQEI LEVGASRPAL
     ESFKAFRGRE PTIDALLRHS GLEAA
//