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Database: UniProt
Entry: B1LVC3
LinkDB: B1LVC3
Original site: B1LVC3 
ID   AMPA_METRJ              Reviewed;         503 AA.
AC   B1LVC3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   29-OCT-2014, entry version 40.
DE   RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE            Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181};
DE            EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181};
DE   AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
GN   Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181};
GN   OrderedLocusNames=Mrad2831_0557;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM
OS   2831).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Presumably involved in the processing and regular
CC       turnover of intracellular proteins. Catalyzes the removal of
CC       unsubstituted N-terminal amino acids from various peptides.
CC       {ECO:0000255|HAMAP-Rule:MF_00181}.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC       Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC       including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC       acid amides and methyl esters are also readily hydrolyzed, but
CC       rates on arylamides are exceedingly low. {ECO:0000255|HAMAP-
CC       Rule:MF_00181}.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC       preferentially leucine, but not glutamic or aspartic acids.
CC       {ECO:0000255|HAMAP-Rule:MF_00181}.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00181}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00181}.
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DR   EMBL; CP001001; ACB22568.1; -; Genomic_DNA.
DR   RefSeq; YP_001753251.1; NC_010505.1.
DR   ProteinModelPortal; B1LVC3; -.
DR   STRING; 426355.Mrad2831_0557; -.
DR   MEROPS; M17.013; -.
DR   EnsemblBacteria; ACB22568; ACB22568; Mrad2831_0557.
DR   GeneID; 6136570; -.
DR   KEGG; mrd:Mrad2831_0557; -.
DR   PATRIC; 22569342; VBIMetRad70578_0584.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243129; -.
DR   KO; K01255; -.
DR   OMA; DSQFADM; -.
DR   OrthoDB; EOG6FV8B3; -.
DR   BioCyc; MRAD426355:GJB5-560-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese;
KW   Metal-binding; Protease; Reference proteome.
FT   CHAIN         1    503       Probable cytosol aminopeptidase.
FT                                /FTId=PRO_1000098330.
FT   ACT_SITE    280    280       {ECO:0000255|HAMAP-Rule:MF_00181}.
FT   ACT_SITE    354    354       {ECO:0000255|HAMAP-Rule:MF_00181}.
FT   METAL       268    268       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       273    273       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       273    273       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       291    291       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       350    350       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       352    352       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       352    352       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
SQ   SEQUENCE   503 AA;  52045 MW;  D9D18D92C6B47F0F CRC64;
     MADGIEIGFG PLEQSGQGPG GSGDLVVFVG DDLSLGSAAR EALGASGADL VARAAASEKF
     KGRSLSALSL PAPAGVGADR LVVVGLGSEK DRAKTDWPAL GGFTASKVAG RTARVVLDWP
     GTTVTAAQAG EFALGARLRT YAFDRYKTKK KPDADDKSVT ALTLLLADHG AAAREGEGAR
     SLSDGVILAR DLVNEPPNVL FPAEFARRAS ELAKLGVEIE VLEPARMREL GMGALLAVAQ
     GSAREPRIVI MRWNGGPAAE APVALIGKGV VFDSGGVSIK PGGGMEDMKG DMGGAAAVVG
     ALHALAARKA RCNVVGAIGI VENMPDGGAY RPSDILTSMS GQTIEVINTD AEGRLVLADV
     ITHVIRSTKP KAIVDLATLT GAIIVALGQD IAGMFSNDDT LASNIHAAGE ATGEKVWRMP
     LIPAYDKAID SKFADMKNTG GRHGGAATAA SFIKRYVEDV PWAHLDIAGV AMSSNASEIN
     RSWGAGWGVR LLDRLIRDHY EAR
//
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