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Database: UniProt/SWISS-PROT
Entry: AMPA_SALEP
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Original site: AMPA_SALEP 
ID   AMPA_SALEP              Reviewed;         503 AA.
AC   B5R1K2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   01-OCT-2014, entry version 38.
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=SEN4230;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K.,
RA   Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A.,
RA   Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G.,
RA   Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and
RT   Salmonella gallinarum 287/91 provides insights into evolutionary and
RT   host adaptation pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933172; CAR35785.1; -; Genomic_DNA.
DR   RefSeq; YP_002246254.1; NC_011294.1.
DR   ProteinModelPortal; B5R1K2; -.
DR   SMR; B5R1K2; 1-503.
DR   STRING; 550537.SEN4230; -.
DR   PRIDE; B5R1K2; -.
DR   EnsemblBacteria; CAR35785; CAR35785; SEN4230.
DR   PATRIC; 32339187; VBISalEnt14964_4306.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243132; -.
DR   OMA; ANEAKMS; -.
DR   OrthoDB; EOG6FV8B3; -.
DR   BioCyc; SENT550537:GJFI-4292-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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    503       Probable cytosol aminopeptidase.
FT                                /FTId=PRO_1000098345.
FT   ACT_SITE    282    282       {ECO:0000255|HAMAP-Rule:MF_00181}.
FT   ACT_SITE    356    356       {ECO:0000255|HAMAP-Rule:MF_00181}.
FT   METAL       270    270       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       275    275       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       275    275       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       293    293       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       352    352       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       354    354       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
FT   METAL       354    354       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00181}.
SQ   SEQUENCE   503 AA;  54890 MW;  65649F32506FA00A CRC64;
     MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
     LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
     NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI
     AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMRE LGMNAYLAVG
     HGSQNESLMS VIEYKGNPSE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
     YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
     DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMSNHN PLAHELIGAS EQAGDRAWRL
     PLGDEFQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
     ATGRPVALLS QFLLNRAGFN GEE
//
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