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 01-MAY-2013, entry version 33.
DE RecName: Full=Probable cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; 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 (By
CC similarity).
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.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC preferentially leucine, but not glutamic or aspartic acids.
CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
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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; M17.003; -.
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; NMHLMRY; -.
DR ProtClustDB; CLSK2331797; -.
DR BioCyc; MRAD426355:GJB5-560-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 PANTHER; PTHR11963:SF3; PTHR11963:SF3; 1.
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.
FT CHAIN 1 503 Probable cytosol aminopeptidase.
FT /FTId=PRO_1000098330.
FT ACT_SITE 280 280 Potential.
FT ACT_SITE 354 354 Potential.
FT METAL 268 268 Manganese 2 (By similarity).
FT METAL 273 273 Manganese 1 (By similarity).
FT METAL 273 273 Manganese 2 (By similarity).
FT METAL 291 291 Manganese 2 (By similarity).
FT METAL 350 350 Manganese 1 (By similarity).
FT METAL 352 352 Manganese 1 (By similarity).
FT METAL 352 352 Manganese 2 (By similarity).
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
//
