ID J2RNV3_9PSED Unreviewed; 683 AA.
AC J2RNV3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=PMI29_05092 {ECO:0000313|EMBL:EJM56316.1};
OS Pseudomonas sp. GM49.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144331 {ECO:0000313|EMBL:EJM56316.1, ECO:0000313|Proteomes:UP000007288};
RN [1] {ECO:0000313|EMBL:EJM56316.1, ECO:0000313|Proteomes:UP000007288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM49 {ECO:0000313|EMBL:EJM56316.1,
RC ECO:0000313|Proteomes:UP000007288};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM56316.1}.
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DR EMBL; AKJL01000272; EJM56316.1; -; Genomic_DNA.
DR RefSeq; WP_008002252.1; NZ_AKJL01000272.1.
DR AlphaFoldDB; J2RNV3; -.
DR MEROPS; M03.004; -.
DR PATRIC; fig|1144331.3.peg.4855; -.
DR Proteomes; UP000007288; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 29..150
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 225..676
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 683 AA; 75457 MW; 5226A3737319E51C CRC64;
MSVNNPLLQS YDLPPFSAIR AEHVQPAIEQ ILADNRAAIV EILKTQAKQP TWAGLVLAMD
ELNDRLGAAW SPVSHLNAVC NSAELREAYE SCLPALSAYA TELGQNRELF QAFEALASSP
QAAGFDVAQK TILEHSLRDF RLSGIDLPEA EQKRYAEVQS KLSELGSRFS NQLLDATQAW
TKHITDEAAL AGLTDSAKAQ MAAAAQAKDL DGWLITLEFP SYYAVMTYAQ DRALREEVYA
AYCTRASDQG PNAGQNDNGP VMEEILDLRQ ELAKLLGFSS FSELSLATKM AESSDQVLSF
LRDLAKRSKP FATQDLEQLK AYAAGQGCPD LQSWDSGFYG EKLREQRYSV AQEALRAYFP
IDKVLSGLFA IVQRLYGIEI AELKGFDTWH PDVRLFEIKE NGQHVGRFFF DLYARANKRG
GAWMDGARDR RRTAGGVLQS PVANLVCNFT PADSGKPALL THDEVTTLFH EFGHGLHHLL
TRVEHAGASG INGVAWDAVE LPSQFMENWC WEPEGLALIS GHYESGEPLP QDLLGKMLAA
KNFQSGLMMV RQLEFSLFDF ELHATHGDGR SVLQVLEGVR DEVSVMRPPA YNRFPNSFAH
IFAGGYAAGY YSYKWAEVLS ADAFSKFEEE GVLNADTGRA FREAILARGG SQEPMVLFVD
FRGREPSIDA LLRHSGLSED AAA
//
