ID A0A0M2ZB89_9MYCO Unreviewed; 420 AA.
AC A0A0M2ZB89;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 28-MAR-2018, entry version 18.
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=BST23_12525 {ECO:0000313|EMBL:ORA65825.1};
OS Mycobacterium elephantis.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=81858 {ECO:0000313|EMBL:ORA65825.1, ECO:0000313|Proteomes:UP000192772};
RN [1] {ECO:0000313|EMBL:ORA65825.1, ECO:0000313|Proteomes:UP000192772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FI-09383 {ECO:0000313|EMBL:ORA65825.1,
RC ECO:0000313|Proteomes:UP000192772};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:ORA65825.1}.
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DR EMBL; MVHP01000012; ORA65825.1; -; Genomic_DNA.
DR RefSeq; WP_046753838.1; NZ_MVHP01000012.1.
DR EnsemblBacteria; KKW62876; KKW62876; AAV95_20140.
DR Proteomes; UP000192772; 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 Gene3D; 2.30.250.10; -; 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; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ORA65825.1};
KW Complete proteome {ECO:0000313|Proteomes:UP000192772};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW ECO:0000256|RuleBase:RU004386};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT METAL 75 75 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT METAL 149 149 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT METAL 395 395 Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ SEQUENCE 420 AA; 44815 MW; E0FEA3DCEA9CEB86 CRC64;
MSASPRGLCE FIDASPSPYH VCETVAERLR AAGFSELAED DAWPAQGRFF SVRAGSLIAW
RTGEPGLPFR IVGAHTDSPN LRVKQHPDRV VAGWQVVALQ PYGGAWLNSW LDRDLGISGR
LSVYDGDRLV HPLVRIDEPI LRVPQLAIHL AEDRKAVALD PQRHVNAVWG VGSEPRSFLG
YVAQRAGVDP ADVLGADLMT HDLTPARLIG ADGELLSAPR LDNQASCYAG LEAFLAASEA
GPSGYLPVLV LFDHEEVGSQ SAHGAQSDLL LTVLERITLS EGGGREEFLR RLPGSMVASG
DMAHATHPNY PERHEPGHLI EVNAGPVLKV QPNLRYATDG RTAAAFALAC AQAGVPLQRY
EHRADLPCGS TIGPMTSART GIPTVDVGAP QLAMHSAREV MGAEDVAAYA AALQAFLAPA
//
