ID   OPDA_HAEIN              Reviewed;         681 AA.
AC   P44573;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Oligopeptidase A;
DE            EC=3.4.24.70;
GN   Name=prlC; OrderedLocusNames=HI_0214;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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) (By similarity). {ECO:0000250}.
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; L42023; AAC21882.1; -; Genomic_DNA.
DR   PIR; C64055; C64055.
DR   RefSeq; NP_438383.2; NC_000907.1.
DR   AlphaFoldDB; P44573; -.
DR   SMR; P44573; -.
DR   STRING; 71421.HI_0214; -.
DR   MEROPS; M03.004; -.
DR   EnsemblBacteria; AAC21882; AAC21882; HI_0214.
DR   KEGG; hin:HI_0214; -.
DR   PATRIC; fig|71421.8.peg.219; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_1_6; -.
DR   OrthoDB; 9773538at2; -.
DR   PhylomeDB; P44573; -.
DR   Proteomes; UP000000579; 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; 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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..681
FT                   /note="Oligopeptidase A"
FT                   /id="PRO_0000078161"
FT   ACT_SITE        471
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         470
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         474
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         477
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   681 AA;  78017 MW;  1452905A001ECFC5 CRC64;
     MSMSNPLLNI QGLPPFSQIK PEHIRPAVEK LIQDCRNTIE QVLKQPHFTW ENFILPLTET
     NDRLNRAWSP VSHLNSVKNS TELREAYQTC LPLLSEYSTW VGQHKGLYNA YLALKNSAEF
     ADYSIAQKKA IENSLRDFEL SGIGLSEEKQ QRYGEIVARL SELNSQFSNN VLDATMGWEK
     LIENEAELAG LPESALQAAQ QSAESKGLKG YRFTLEIPSY LPVMTYCENR ALREEMYRAY
     ATRASEQGPN AGKWDNSKVM EEILTLRVEL AKLLGFNTYT ELSLATKMAE NPQQVLDFLD
     HLAERAKPQG EKELQELKGY CEKEFGVTEL APWDIGFYSE KQKQHLYAIN DEELRPYFPE
     NRVISGLFEL IKRIFNIRAV ERKGVDTWHK DVRFFDLIDE NDQLRGSFYL DLYAREHKRG
     GAWMDDCIGR KRKLDGSIET PVAYLTCNFN APIGNKPALF THNEVTTLFH EFGHGIHHML
     TQIDVSDVAG INGVPWDAVE LPSQFMENWC WEEEALAFIS GHYETGEPLP KEKLTQLLKA
     KNFQAAMFIL RQLEFGIFDF RLHHTFDAEK TNQILDTLKS VKSQVAVIKG VDWARAPHSF
     SHIFAGGYAA GYYSYLWAEV LSADAYSRFE EEGIFNPITG KSFLDEILTR GGSEEPMELF
     KRFRGREPQL DALLRHKGIM N
//