ID Q65TA4_MANSM Unreviewed; 679 AA.
AC Q65TA4;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN Name=dcp {ECO:0000313|EMBL:AAU37806.1};
GN OrderedLocusNames=MS1199 {ECO:0000313|EMBL:AAU37806.1};
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU37806.1, ECO:0000313|Proteomes:UP000000607};
RN [1] {ECO:0000313|EMBL:AAU37806.1, ECO:0000313|Proteomes:UP000000607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU37806.1,
RC ECO:0000313|Proteomes:UP000000607};
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37806.1; -; Genomic_DNA.
DR RefSeq; WP_011200373.1; NC_006300.1.
DR AlphaFoldDB; Q65TA4; -.
DR STRING; 221988.MS1199; -.
DR MEROPS; M03.004; -.
DR KEGG; msu:MS1199; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_1_6; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000000607; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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.
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 26..147
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 221..676
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 679 AA; 77306 MW; 74B8F139CDA33DF5 CRC64;
MSNPLLENTP LPQFSKIKPE HIQPAIEQLI QDCRITTENL LKQPQLSWDN FCQPLSEVND
RLSKAWSPVS HLNSVKNSNE LRDAYQACLP MLSEYGTWVG QHQGLYNAYV QLKNSPEFAG
YSPAQKKAVE NSLRDFKLSG ISLAPEQQKR YGEIVSRLSE LSSQFSNNVL DATMGWDKVI
TDEEQLKGLP ESALQAAKQS AQNKGVEGYR FTLEFPSYIP VMTYCENREL REEMYRAFVT
RASDQGPNAG KWDNSAIMEE ILTLRVELAK LLGFNSYTEL SLATKMAETP AQVLSFLDDL
AMRSKPQGEK ELADLYAFCE KEFAITELEP WDISYYSEKE KQALYAINDE ELRPYFPEQR
VISGLFELIK RIFNIRAVER QGVDCWHKDV RFFDLIDETD EVRGSFYLDL YAREHKRGGA
WMDDCIGRKI KADGALQKPV AYLTCNFNAP VGDKPALFTH DEVTTLFHEF GHGIHHMLTK
VDIGDVSGIN GVPWDAVELP SQFMENWCWE EEALAFISGH YQTGEPLPKE KLTQLLKAKN
FHAAMFVLRQ LEFGIFDFRL HDNYKPGKAN QILDTLNAVK DQVSVVKAVD WARTPHSFGH
IFSGGYAAGY YSYLWAEVLS ADAFSRFEEE GIFNAVTGKS YLDEILTKGG SEEPMVLFER
FRGRKPTLDA LLRHKGIAN
//
