ID A0A0A1HW77_9PSED Unreviewed; 683 AA.
AC A0A0A1HW77;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, 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=BN844_4489 {ECO:0000313|EMBL:CDF94495.1};
OS Pseudomonas sp. SHC52.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF94495.1, ECO:0000313|Proteomes:UP000031550};
RN [1] {ECO:0000313|EMBL:CDF94495.1, ECO:0000313|Proteomes:UP000031550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SHC52 {ECO:0000313|EMBL:CDF94495.1,
RC ECO:0000313|Proteomes:UP000031550};
RA Van der Voort M., Mendes R., Raaijmakers J.M.;
RT "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL Submitted (MAY-2013) 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:CDF94495.1}.
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DR EMBL; CBLV010000195; CDF94495.1; -; Genomic_DNA.
DR RefSeq; WP_041022247.1; NZ_CBLV010000195.1.
DR AlphaFoldDB; A0A0A1HW77; -.
DR MEROPS; M03.004; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000031550; Unassembled WGS sequence.
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; 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..151
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; 75718 MW; EE33D944C2683AAB CRC64;
MSVNNPLLQP YDLPPFSAIR AEHVQPAIEQ ILADNRAAIA QILKTQGQQP SWAGLVLAMD
ELNDRLGAAW SPVSHLNAVR NSPELREAYE ACLPALSAYS TELGQNRELF QAFEALASSP
EAAGFDVAQK TILEHSLRDF RLSGIDLPPE QQKRYAEVQS KLSELGSRFS NQLLDATQAW
TKHVTDEAAL AGLTDSAKAQ MAAAAQAKEL DGWLINLEFP SYYAVMTYAE DRALREEVYA
AYCTRASDQG PNAGQNDNGP VMEQILDLRQ ELAQLLGFAN FAELSLATKM AESSDQVLSF
LRDLAKRSKP FAAQDLEQLK AFAAEQGCPD LQSWDSGFYG EKLRQQRYSV AQEALRAYFP
IDKVLSGLFA IVQRLYGIEI AELKGFDAWH PDVRLFEIKE NGQHVGRFFF DLYARANKRG
GAWMDGARDR RRTIDGVLQS PVANLVCNFT PADSGKPALL THDEVTTLFH EFGHGLHHLL
TRVEHAGVSG INGVAWDAVE LPSQFMENWC WEPEGLALIS GHYETGEPLP QDLLEKMLAA
KNFQSGLMMV RQLEFSLFDF ELHATHGDGR SVLQVLEGVR DEVSVMRPPA YNRFPNSFAH
IFAGGYAAGY YSYKWAEVLS ADAFSKFEED GVLNADTGRA FREAILARGG SQEPMVLFVD
FRGREPSIDA LLRHSGLSED AAA
//
