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Database: UniProt/SWISS-PROT
Entry: AMPA_RHIL3
LinkDB: AMPA_RHIL3
Original site: AMPA_RHIL3 
ID   AMPA_RHIL3              Reviewed;         496 AA.
AC   Q1MIZ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   29-OCT-2014, entry version 60.
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}; OrderedLocusNames=RL1571;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R.,
RA   Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D.,
RA   Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C.,
RA   Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A.,
RA   Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and
RT   accessory components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK07066.1; -; Genomic_DNA.
DR   RefSeq; YP_767175.1; NC_008380.1.
DR   ProteinModelPortal; Q1MIZ4; -.
DR   STRING; 216596.RL1571; -.
DR   MEROPS; M17.003; -.
DR   EnsemblBacteria; CAK07066; CAK07066; RL1571.
DR   GeneID; 4401650; -.
DR   KEGG; rle:RL1571; -.
DR   PATRIC; 23139675; VBIRhiLeg32091_2779.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243129; -.
DR   KO; K01255; -.
DR   OMA; AMELGFP; -.
DR   OrthoDB; EOG6FV8B3; -.
DR   BioCyc; RLEG216596:GKE5-1603-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.
FT   CHAIN         1    496       Probable cytosol aminopeptidase.
FT                                /FTId=PRO_1000019966.
FT   ACT_SITE    274    274       {ECO:0000255|HAMAP-Rule:MF_00181}.
FT   ACT_SITE    348    348       {ECO:0000255|HAMAP-Rule:MF_00181}.
FT   METAL       262    262       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       267    267       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       267    267       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       285    285       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       344    344       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       346    346       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       346    346       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
SQ   SEQUENCE   496 AA;  52209 MW;  76271929591BBD3D CRC64;
     MSIKLEISFS KSAKLNGGLA ILLKTAEADS AAGAETVDPA GVIVKAARIA RYSAKSMNGL
     DIVVPEGAPV DRIVVIGLGK AAELTAHDWL KAGGAAASRI KNTDKAAVFI DVPGLTTSPR
     AAADFALGML LRAYSFDTYK TKKGDEEEKP AKSVKVTIVT ADPAGAKKAF SDSEAIAGGV
     NLARDLVNEP PNVLGPVEFA AKAKELEKLG VEVEILTERE MRRLGMGALL GVAQGSVRPP
     RLAVMQWKGG KGKDRPVAFI GKGVVFDTGG ISIKPAAGME DMKGDMGGAA AVTGLMHVLA
     SRKAAVNAVG IIGLVENMPD GNAQRPGDIV TSMSGQTIEV INTDAEGRLV LCDALWYCND
     RFKPQFMINL ATLTGAIIVA LGNVHAGLFS NDDQLSAQLT AAGLSSNEKL WRMPLGRDYD
     KLIDSKFADM KNTGGRQAGS ITAAHFLKRF VQDTPWAHLD IAGTAMGSPQ DEINQSWGSG
     FGVRLLDELV RAHYES
//
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