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Database: UniProt/TrEMBL
Entry: B7LTI2_ESCF3
LinkDB: B7LTI2_ESCF3
Original site: B7LTI2_ESCF3 
ID   B7LTI2_ESCF3            Unreviewed;       702 AA.
AC   B7LTI2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAQ91041.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAQ91041.1};
GN   Name=malS {ECO:0000313|EMBL:CAQ91041.1};
GN   OrderedLocusNames=EFER_3569 {ECO:0000313|EMBL:CAQ91041.1};
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ91041.1, ECO:0000313|Proteomes:UP000000745};
RN   [1] {ECO:0000313|Proteomes:UP000000745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73
RC   {ECO:0000313|Proteomes:UP000000745};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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DR   EMBL; CU928158; CAQ91041.1; -; Genomic_DNA.
DR   ProteinModelPortal; B7LTI2; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAQ91041; CAQ91041; EFER_3569.
DR   KEGG; efe:EFER_3569; -.
DR   HOGENOM; HOG000273912; -.
DR   KO; K01176; -.
DR   OMA; DKVMVVW; -.
DR   OrthoDB; POG091H07J7; -.
DR   Proteomes; UP000000745; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030980; P:alpha-glucan catabolic process; IEA:InterPro.
DR   GO; GO:0051692; P:cellular oligosaccharide catabolic process; IEA:InterPro.
DR   InterPro; IPR014635; A_amylase_MalS.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF036917; Alph_amls_MalS; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000745};
KW   Glycosidase {ECO:0000313|EMBL:CAQ91041.1};
KW   Hydrolase {ECO:0000313|EMBL:CAQ91041.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     43       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        44    702       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002857538.
FT   DOMAIN      219    663       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   702 AA;  79300 MW;  A699916F4643D35B CRC64;
     MITREEFYRT YHWQTGEIRS NKSSSIMKLA ACFLLLLPGV AVAATWTSGG FPTFDEQSTG
     KYASHAQLTK GTRALTLNFD QQCWQPADAI KLNQMLSLKP CDSTPPQWRL FRDGEYTLQV
     DTRSGTPTLM ISVTSTAQPT INLIRECPKW DGQPLTLDVS QTFPEGAAIR EYYSQQIVTV
     KNGHITLKPV TESNGLLLLE HAETHTSAPF DWHNATVYFV LTDRFENGDP GNDQSYGRHK
     DGMQEIGTFH GGDLRGLTNK LDYLQQLGVN ALWISAPFEQ IHGWVGGGTK GDFPHYAYHG
     YYTQDWTNLD ANIGSEAELR ALVDGAHQRG IRIIFDVVMN HTGYATLADM QEFQFGALYL
     SGDELKKTLG ERWSDWKPAA GQTWHSFNDY INFSDKTGWE KWWGKNWIRT DIGDYDNPGF
     DDLTMSLAFL PDIKTESTTA SGLPVFYKNK PDTHAKAIDG YTPRDYLTHW LSQWVRDYGI
     DGFRVDTAKH VELPAWQQLK TEASAALNEW KKANPEKALD DNSFWMTGEA WGHGVMQSDY
     YRNGFDAMIN FDYQEQAAKA VDCLAQMDNI WQQMAEKLQD FNVLSYLSSH DTRLFREGGK
     KSAELLLLAP GAVQIFYGDE SLRPFGPTGS DPLQGTRSDM NWQDVSDKSA ASVKHWQRIS
     QFRARHLAIG AGKQTTLSLP QGYGFVREHG DDKVMVIWAG QH
//
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