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Database: UniProt/SWISS-PROT
Entry: AMPA_ECOL5
LinkDB: AMPA_ECOL5
Original site: AMPA_ECOL5 
ID   AMPA_ECOL5              Reviewed;         503 AA.
AC   Q0T9D1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   01-OCT-2014, entry version 55.
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=ECP_4509;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG72448.1; -; Genomic_DNA.
DR   RefSeq; YP_672349.1; NC_008253.1.
DR   ProteinModelPortal; Q0T9D1; -.
DR   SMR; Q0T9D1; 1-503.
DR   STRING; 362663.ECP_4509; -.
DR   PRIDE; Q0T9D1; -.
DR   EnsemblBacteria; ABG72448; ABG72448; ECP_4509.
DR   GeneID; 4188573; -.
DR   KEGG; ecp:ECP_4509; -.
DR   PATRIC; 18199968; VBIEscCol77757_4559.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243132; -.
DR   KO; K01255; -.
DR   OMA; ANEAKMS; -.
DR   OrthoDB; EOG6FV8B3; -.
DR   BioCyc; ECOL362663:GIY5-4551-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_1000019915.
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;  54880 MW;  643DED17EAC44DCD CRC64;
     MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
     LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
     NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI
     AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG
     QGSQNESLMS VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
     YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
     DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL
     PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
     ATGRPVALLA QFLLNRAGFN GEE
//
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