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Database: UniProt/TrEMBL
Entry: B7MES8_ECO45
LinkDB: B7MES8_ECO45
Original site: B7MES8_ECO45 
ID   B7MES8_ECO45            Unreviewed;       676 AA.
AC   B7MES8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   22-NOV-2017, entry version 56.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAR05199.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAR05199.1};
GN   Name=malS {ECO:0000313|EMBL:CAR05199.1};
GN   OrderedLocusNames=ECS88_3990 {ECO:0000313|EMBL:CAR05199.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR05199.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
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; CU928161; CAR05199.1; -; Genomic_DNA.
DR   RefSeq; WP_000761248.1; NC_011742.1.
DR   ProteinModelPortal; B7MES8; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAR05199; CAR05199; ECS88_3990.
DR   KEGG; ecz:ECS88_3990; -.
DR   HOGENOM; HOG000273912; -.
DR   KO; K01176; -.
DR   OMA; DKVMVVW; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); 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:UP000000747};
KW   Glycosidase {ECO:0000313|EMBL:CAR05199.1};
KW   Hydrolase {ECO:0000313|EMBL:CAR05199.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    676       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002860445.
FT   DOMAIN      193    637       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   676 AA;  75772 MW;  C1E560649F274D34 CRC64;
     MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
     ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQLDTRSGT PTLMISLQNT VEPVASLVRE
     CPKWDGLPLT LDVSATFAEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDT
     SAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
     LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGSE ADLRTLVDSA
     HQRGIRILFD IVMNHTGYAT LADMQEYQFG ALYLSGDELK KTLGERWSDW KPAAGQTWHS
     FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
     YKNKTDTHAK VIDGFTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA
     LREWKKANPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
     MDTTWQQMAE KLQDFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
     PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
     REHGDDKVLV IWAGQQ
//
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