ID A0A0J5P6Y6_9PAST Unreviewed; 677 AA.
AC A0A0J5P6Y6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=RO21_05895 {ECO:0000313|EMBL:KMK51535.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK51535.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK51535.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK51535.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK51535.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JWIZ01000031; KMK51535.1; -; Genomic_DNA.
DR RefSeq; WP_047976872.1; NZ_JWIZ01000031.1.
DR AlphaFoldDB; A0A0J5P6Y6; -.
DR STRING; 67855.RO21_05895; -.
DR PATRIC; fig|67855.3.peg.1158; -.
DR Proteomes; UP000036270; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000036270};
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..674
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 677 AA; 76933 MW; E5DCBAEF13589870 CRC64;
MTNPLLNATC LPRFSQIKPE HIEPAVRELL QQCRQTIEQV AQIAEPTWEN FYLPQAMAGD
RLSRAWSPVG HLNAVKNSPE LREAYQACLP LLSEYSTWAG QHQGLYQGYL KLKNSPAFEH
YSIAQKKAVE NSLRDFELSG ISLSPEKQQR YGEISMRLSE LSAQFSNNVL DATMGWEIVI
DNEADLAGLS ESALEAAKLS AQSKDKNGYR FTLEFPSYLP VMTYCENRSL REKMYQAFNT
RASDQGENAG KWDNSAIMAE TLALRLELAQ LLGFETYADY SLATKMAESP KQVIDFLEDL
ANRSKAQGEK ELAALREFAE KNYGVSELAP WDIAFYSEKQ KQALYAINDE ELRPYFPEDR
VLSGLFELIK RIFGMRVVEQ SEFDSYHDDV RFFTIFDETD RLRGSFYLDL YAREHKRGGA
WMDDCINQKR LADGTLQKPV AYLTCNFNKP LGDKPALFTH DEVTTLFHEF GHGIHHMLTE
IEVGDVAGIN GVPWDAVELP SQFLENWCWE EEALAFISGH YETGEPLPKA KLTQLLKAKN
YQAAMFVLRQ LEFGLFDLRL HLAAPKANIV LDTLQAVKSQ VALIKTPDWV RTPHSFSHIF
AGGYAAGYYS YLWAEVLSAD AYARFEEEGI FSRTVGQAFL DHILTRGGSE EPMVLFERFR
GRKPTLDALL RHKGIAN
//
