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Database: UniProt
Entry: Q328S1
LinkDB: Q328S1
Original site: Q328S1 
ID   AMPA_SHIDS              Reviewed;         503 AA.
AC   Q328S1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   26-NOV-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};
GN   OrderedLocusNames=SDY_4284;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC       Note=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; CP000034; ABB64184.1; -; Genomic_DNA.
DR   RefSeq; YP_405675.1; NC_007606.1.
DR   ProteinModelPortal; Q328S1; -.
DR   SMR; Q328S1; 1-503.
DR   STRING; 300267.SDY_4284; -.
DR   MEROPS; M17.003; -.
DR   EnsemblBacteria; ABB64184; ABB64184; SDY_4284.
DR   GeneID; 3796952; -.
DR   KEGG; sdy:SDY_4284; -.
DR   PATRIC; 18699398; VBIShiDys99784_5050.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243132; -.
DR   KO; K01255; -.
DR   OMA; ANEAKMS; -.
DR   OrthoDB; EOG6FV8B3; -.
DR   BioCyc; SDYS300267:GJEW-4280-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_1000019981.
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;  54866 MW;  BF94CC87F859C2C0 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 QLPVNVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
     DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL
     PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
     ATGRPVALLA QFLLNRAGFN GEE
//
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