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
//
