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Database: UniProt
Entry: L0J5F4_9MYCO
LinkDB: L0J5F4_9MYCO
Original site: L0J5F4_9MYCO 
ID   L0J5F4_9MYCO            Unreviewed;       421 AA.
AC   L0J5F4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-NOV-2017, entry version 35.
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=Mycsm_05640 {ECO:0000313|EMBL:AGB25817.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB25817.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) 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}.
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DR   EMBL; CP003078; AGB25817.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; AGB25817; AGB25817; Mycsm_05640.
DR   KEGG; msa:Mycsm_05640; -.
DR   PATRIC; fig|710686.3.peg.5682; -.
DR   KO; K01267; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000010844; Chromosome.
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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:AGB25817.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010844};
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        79     79       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       153    153       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       396    396       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   421 AA;  44848 MW;  35808E20E5BBB216 CRC64;
     MGISGASAQG LCEFIDASPS PFHVCATAAL RLVDAGFTEL SEADAWPASG RFFTVRAGSL
     VAWIAGGDAN APFRIVGAHT DSPNLRVKQH PDRFVSGWQV VALQPYGGAW LNSWLDRDLG
     VSGRLSLRVG NTLDHWLVRI DEPILRVPQL AIHLAEDRKA VSLDPQRHVN AVWGVGSGSR
     SFLRYVAEHA GVAEADVLGF DLMTHDLTPS RLGGVNQELV SAPRLDNQAT CYAGLEALLA
     VEPTDHVPVL ALFDHEEVGS QSDHGAQSEL LPTVLERITL AARGSREDFL RRASTSMVAS
     GDMAHATHPN YPERHEPGHL IEVNAGPVVK VQPNLRYATD GRTAAAFALA CAQAGVPLQR
     YEHRADLPCG STIGPMTSAR TGIPTVDVGA PQLAMHSARE VMGAADVAAY SAALQAFLSP
     L
//
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