ID A0A0N0JVI6_9PROT Unreviewed; 676 AA.
AC A0A0N0JVI6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=IP84_07205 {ECO:0000313|EMBL:KPF68976.1};
OS beta proteobacterium AAP99.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF68976.1, ECO:0000313|Proteomes:UP000037960};
RN [1] {ECO:0000313|EMBL:KPF68976.1, ECO:0000313|Proteomes:UP000037960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP99 {ECO:0000313|EMBL:KPF68976.1,
RC ECO:0000313|Proteomes:UP000037960};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF68976.1}.
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DR EMBL; LJIA01000006; KPF68976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0JVI6; -.
DR STRING; 1523428.IP84_07205; -.
DR PATRIC; fig|1523428.3.peg.3004; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000037960; 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; 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; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 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:UP000037960};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 30..149
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 222..671
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 676 AA; 75346 MW; 135BB3D75013CF09 CRC64;
MSTNPLLDFS DLPRFAEIRP EHVTPALDAL LPTAQAAVDA VATGSGCTWA QVVEPLNEPL
ERLSRAWGLV GHLQAVVDTP ELRAAYNDNL PRVTEFYTNL NADLRLFERY KAIASDAGYA
SLSAERKTVV EHALRDFRLG GAELTGEKRE RFAAIAARLA EISQKFSEHL LDATNAWSLL
ITDATELRGL PQDALDAAAE AAKADGKDGY KLTLHIPSYL PVMQYCENRS LRETVYRAYV
TRASELADPA QDNSAFMVEI LALRDEQAKL LGYPHHAALS LVPKMAQSAE QVIDFVRDMA
RRAKPYAEKD MAEICDFGRA ALGIADVQAW DVAFISEKLR LARYSYSDTE VKQYFTEPQV
MDGLFKVIGT LFDVQIDKVD GPVWHGDVRL YRFARKGEAL AHVYVDNYAR NGKRGGAWMD
VCRVRRQLAS QLQTPVAYVN CNFASPVGGK PALLTHDDVI TLFHEYGHAL HHLLTQVNEP
GADMRAVEWD AIELPSQFME NFCWEWDVVR GMTRHVDSGE PLPRALFDKM LAAKNFQAGM
QSVRQMEFAL FDMRLHSETP APTAAAVQQV IDEVRAEVAV ITPPAFNRFQ HSFSHIFAGG
YSAGYYSYKW AEVMSADAFS LFEETGTLNP DTGRKFRDEV LAVGATRPAA ESFRAFRGRD
PQPDALLRHY GMLAAA
//
