ID   OPDA_SALTY              Reviewed;         680 AA.
AC   P27237;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Oligopeptidase A;
DE            EC=3.4.24.70;
GN   Name=prlC; Synonyms=opdA, optA; OrderedLocusNames=STM3594;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RX   PubMed=1537805; DOI=10.1128/jb.174.5.1631-1640.1992;
RA   Conlin C.A., Miller C.G.;
RT   "Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase
RT   A in Salmonella typhimurium.";
RL   J. Bacteriol. 174:1631-1640(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: May play a specific role in the degradation of signal
CC       peptides after they are released from precursor forms of secreted
CC       proteins. Can cleave N-acetyl-L-Ala(4).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; M84574; AAA27172.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22454.1; -; Genomic_DNA.
DR   PIR; A42298; A42298.
DR   RefSeq; NP_462495.1; NC_003197.2.
DR   RefSeq; WP_000184178.1; NC_003197.2.
DR   AlphaFoldDB; P27237; -.
DR   SMR; P27237; -.
DR   STRING; 99287.STM3594; -.
DR   MEROPS; M03.004; -.
DR   PaxDb; P27237; -.
DR   EnsemblBacteria; AAL22454; AAL22454; STM3594.
DR   GeneID; 1255117; -.
DR   KEGG; stm:STM3594; -.
DR   PATRIC; fig|99287.12.peg.3798; -.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   OMA; KNFQSAM; -.
DR   PhylomeDB; P27237; -.
DR   BioCyc; SENT99287:STM3594-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   Gene3D; 1.20.1050.40; -; 1.
DR   Gene3D; 3.40.390.10; -; 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; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF19310; TOP_N; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Zinc.
FT   CHAIN           1..680
FT                   /note="Oligopeptidase A"
FT                   /id="PRO_0000078160"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   680 AA;  76944 MW;  CA0F11C80FE13F89 CRC64;
     MTNPLLTSFS LPPFSAIKPE HVVPAVTKAL ADCRAAVEGV VAHGAPYSWE NLCQPLAEAD
     DVLGRIFSPI SHLNSVKNSP ELREAYEQTL PLLSEYSTWV GQHEGLYNAY RDLRDGDHYA
     TLNTAQKKAV DNALRDFELS GIGLPKEKQQ RYGEIATRLS ELGNQYSNNV LDATMGWTKL
     ITDEAELAGM PESALAAAKA QAEAKEQEGY LLTLDIPSYL PVMTYCDNQA LREEMYRAYS
     TRASDQGPNA GKWDNSPVME EILALRHELA QLLGFENYAH ESLATKMAEN PQQVLDFLTD
     LAKRARPQGE KELAQLRAFA KAEFGVEELQ PWDIAYYSEK QKQHLYSISD EQLRPYFPEN
     KAVNGLFEVV KRIYGITAKE RTDVDVWHPE VRFFELYDEN NELRGSFYLD LYAREHKRGG
     AWMDDCVGQM RKADGTLQKP VAYLTCNFNR PVNGKPALFT HDEVITLFHE FGHGLHHMLT
     RIETAGVSGI SGVPWDAVEL PSQFMENWCW EPEALAFISG HYETGEPLPK ELLDKMLAAK
     NYQAALFILR QLEFGLFDFR LHAEFNPQQG AKILETLFEI KKQVAVVPSP TWGRFPHAFS
     HIFAGGYAAG YYSYLWADVL AADAYSRFEE EGIFNRETGQ SFLDNILTRG GSEEPMELFK
     RFRGREPQLD AMLEHYGIKG