ID B4F015_PROMH Unreviewed; 680 AA.
AC B4F015;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN Name=prlC {ECO:0000313|EMBL:CAR45919.1};
GN OrderedLocusNames=PMI3005 {ECO:0000313|EMBL:CAR45919.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR45919.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR45919.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR45919.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45919.1; -; Genomic_DNA.
DR RefSeq; WP_012368587.1; NC_010554.1.
DR AlphaFoldDB; B4F015; -.
DR MEROPS; M03.004; -.
DR EnsemblBacteria; CAR45919; CAR45919; PMI3005.
DR GeneID; 6801935; -.
DR KEGG; pmr:PMI3005; -.
DR PATRIC; fig|529507.6.peg.2937; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_1_6; -.
DR Proteomes; UP000008319; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 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; 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..148
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 222..677
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 680 AA; 76877 MW; 3B55CCEF31A74D09 CRC64;
MSNPLLSTTG LPAFSQIEPK HVVPAIKEVL ANYRATVEKL LADNTAFSWD NLCQPLAEAG
DKLSRVWSPV SHLNSVKNSA ELREAYEQSL PLLSEFSTWM GQHEGLYQAY KSIKESADFA
LLTQPQKKAV ENALRDFELS GIGLPKEKQQ RFGEISARLS ELSAKFGNNV LDATMGWSKL
ITDESELAGM PQSAIDAAKA MAQAKEQQGY LLTLDMPSYL PVMTYADNRE LRKEMSIAYS
TRASDQGPNA GQWDNSEVMA EILALRHELA QLLGFKNYAE KSLATKMAES PEQVLNFLTD
LASRAHPQGE KELAELTHFA KTHYGVEKLE PWDLAYYSEK QKQHLFSIDD EQLRPYFPEH
RALSGLFEVV HRIYGLTAKE RHDIDTWHDD VRFFELYDES NTLRGSFYLD LYAREHKRGG
AWMDDCIGRM RHADGTLQNP VAYLTCNFNK PVGDKPALFT HNEVTTLFHE FGHGLHHMLT
QIDTADVSGI NGVPWDAVEL PSQFMENWCW EPEALAFISG HYETGEPLPQ AMLDNMLKAK
NYQSAMFVLR QLEFGLFDFR LHAEYDPAKG ARIMEILNSV KEKVSVVPAT PWARFPHAFS
HIFAGGYAAG YYSYLWADVL AADAFSRFSE EGIFNRQTGQ SFLDNILTRG GSEEPMELFK
RFRGREPKLD AMLKGYGIKG
//
