OPDA_ECOLI
ID OPDA_ECOLI Reviewed; 680 AA.
AC P27298; Q2M7G0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Oligopeptidase A;
DE EC=3.4.24.70;
GN Name=prlC; Synonyms=opdA; OrderedLocusNames=b3498, JW3465;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1325967; DOI=10.1128/jb.174.18.5881-5887.1992;
RA Conlin C.A., Trun N.J., Silhavy T.J., Miller C.G.;
RT "Escherichia coli prlC encodes an endopeptidase and is homologous to the
RT Salmonella typhimurium opdA gene.";
RL J. Bacteriol. 174:5881-5887(1992).
RN [2]
RP SEQUENCE REVISION TO 43.
RX PubMed=8366062; DOI=10.1128/jb.175.17.5731-5732.1993;
RA Conlin C.A., Miller C.G.;
RT "Location of the prlC (opdA) gene on the physical map of Escherichia
RT coli.";
RL J. Bacteriol. 175:5731-5732(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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; M93984; AAA16155.1; -; Unassigned_DNA.
DR EMBL; U00039; AAB18474.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76523.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77796.1; -; Genomic_DNA.
DR PIR; S47718; S47718.
DR RefSeq; NP_417955.1; NC_000913.3.
DR RefSeq; WP_001298719.1; NZ_SSZK01000042.1.
DR AlphaFoldDB; P27298; -.
DR SMR; P27298; -.
DR BioGRID; 4262506; 55.
DR BioGRID; 852324; 1.
DR DIP; DIP-10566N; -.
DR IntAct; P27298; 4.
DR STRING; 511145.b3498; -.
DR MEROPS; M03.004; -.
DR jPOST; P27298; -.
DR PaxDb; P27298; -.
DR PRIDE; P27298; -.
DR EnsemblBacteria; AAC76523; AAC76523; b3498.
DR EnsemblBacteria; BAE77796; BAE77796; BAE77796.
DR GeneID; 948016; -.
DR KEGG; ecj:JW3465; -.
DR KEGG; eco:b3498; -.
DR PATRIC; fig|511145.12.peg.3600; -.
DR EchoBASE; EB1411; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_1_6; -.
DR InParanoid; P27298; -.
DR OMA; KNFQSAM; -.
DR PhylomeDB; P27298; -.
DR BioCyc; EcoCyc:EG11441-MON; -.
DR BioCyc; MetaCyc:EG11441-MON; -.
DR PRO; PR:P27298; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; TAS:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:EcoCyc.
DR GO; GO:0006260; P:DNA replication; TAS:EcoCyc.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IDA:EcoliWiki.
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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..680
FT /note="Oligopeptidase A"
FT /id="PRO_0000078159"
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"
FT CONFLICT 211..212
FT /note="LL -> FV (in Ref. 1; AAA16155)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..266
FT /note="LR -> AA (in Ref. 1; AAA16155)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="D -> H (in Ref. 1; AAA16155)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="S -> T (in Ref. 1; AAA16155)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="A -> G (in Ref. 1; AAA16155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 77167 MW; 41E338F1BFFBF906 CRC64;
MTNPLLTPFE LPPFSKILPE HVVPAVTKAL NDCRENVERV VAQGAPYTWE NLCQPLAEVD
DVLGRIFSPV SHLNSVKNSP ELREAYEQTL PLLSEYSTWV GQHEGLYKAY RDLRDGDHYA
TLNTAQKKAV DNALRDFELS GIGLPKEKQQ RYGEIATRLS ELGNQYSNNV LDATMGWTKL
VTDEAELAGM PESALAAAKA QAEAKELEGY LLTLDIPSYL PVMTYCDNQA LREEMYRAYS
TRASDQGPNA GKWDNSKVME EILALRHELA QLLGFENYAF KSLATKMAEN PQQVLDFLTD
LAKRARPQGE KELAQLRAFA KAEFGVDELQ PWDIAYYSEK QKQHLYSISD EQLRPYFPEN
KAVNGLFEVV KRIYGITAKE RKDVDVWHPD VRFFELYDEN NELRGSFYLD LYARENKRGG
AWMDDCVGQM RKADGSLQKP VAYLTCNFNR PVNGKPALFT HDEVITLFHE FGHGLHHMLT
RIETAGVSGI SGVPWDAVEL PSQFMENWCW EPEALAFISG HYETGEPLPK ELLDKMLAAK
NYQAALFILR QLEFGLFDFR LHAEFRPDQG AKILETLAEI KKLVAVVPSP SWGRFPHAFS
HIFAGGYAAG YYSYLWADVL AADAFSRFEE EGIFNRETGQ SFLDNILSRG GSEEPMDLFK
RFRGREPQLD AMLEHYGIKG
