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Database: UniProt
Entry: A0A0M2ZB89_9MYCO
LinkDB: A0A0M2ZB89_9MYCO
Original site: A0A0M2ZB89_9MYCO 
ID   A0A0M2ZB89_9MYCO        Unreviewed;       420 AA.
AC   A0A0M2ZB89;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
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   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
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
//
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