ID A0A0M8T3C2_9ACTN Unreviewed; 433 AA.
AC A0A0M8T3C2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN ORFNames=ADK56_11090 {ECO:0000313|EMBL:KOU51179.1};
OS Streptomyces sp. MMG1522.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU51179.1, ECO:0000313|Proteomes:UP000037713};
RN [1] {ECO:0000313|EMBL:KOU51179.1, ECO:0000313|Proteomes:UP000037713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1522 {ECO:0000313|EMBL:KOU51179.1,
RC ECO:0000313|Proteomes:UP000037713};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC ECO:0000256|RuleBase:RU004386}.
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:KOU51179.1}.
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DR EMBL; LGDF01000106; KOU51179.1; -; Genomic_DNA.
DR RefSeq; WP_032773512.1; NZ_LGDF01000106.1.
DR AlphaFoldDB; A0A0M8T3C2; -.
DR PATRIC; fig|1415545.3.peg.2387; -.
DR Proteomes; UP000037713; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ SEQUENCE 433 AA; 46018 MW; 23F4ED37E17DA918 CRC64;
MTPAPHRSHT DDLLAFIAAS PSPYHVVASA AQRLEKAGFR ELRGTDDWTG ATGGCFVARA
GALIAWYVPE DAPAHTPFRI VGTHTDSPNL RVKPAPDTGT AGWRQIGVEI YGGVPLNTWL
DRDLGISGRL ALRGPDGVPR NRLVQIDEPL LRVPQLAIHL DRTVNEGVAL DRQRHIAPIW
ALGEPREGEL LRRVASAAGE DPADVLAWDL MLHDVQPPGY LGVDREFVVA SRLDNQVSVH
AGVTALVDAA TGRTRPSYVP VLAAFDHEEV GSGSETGAQS PLLERVLSRS LAARGGSEED
WSRALAGAFC VSADMAHAVH PNYAERHDPD HRPLPNGGPT VKVNVNQRYA TDSTGIAVLT
AAAERAGAPW QPFVSNNAMP CGTSIGPLTA ARLGVTTVDV GVPGLSMHSA REMCGVRDPG
HLAAILTTIM VGE
//
