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Database: UniProt/TrEMBL
Entry: A7ZTB8_ECO24
LinkDB: A7ZTB8_ECO24
Original site: A7ZTB8_ECO24 
ID   A7ZTB8_ECO24            Unreviewed;       676 AA.
AC   A7ZTB8;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   SubName: Full=Alpha-amylase, periplasmic {ECO:0000313|EMBL:ABV20110.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ABV20110.1};
GN   Name=malS {ECO:0000313|EMBL:ABV20110.1};
GN   OrderedLocusNames=EcE24377A_4068 {ECO:0000313|EMBL:ABV20110.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV20110.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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DR   EMBL; CP000800; ABV20110.1; -; Genomic_DNA.
DR   RefSeq; WP_000761263.1; NC_009801.1.
DR   ProteinModelPortal; A7ZTB8; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABV20110; ABV20110; EcE24377A_4068.
DR   KEGG; ecw:EcE24377A_4068; -.
DR   HOGENOM; HOG000273912; -.
DR   KO; K01176; -.
DR   OMA; DKVMVVW; -.
DR   Proteomes; UP000001122; 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:UP000001122};
KW   Glycosidase {ECO:0000313|EMBL:ABV20110.1};
KW   Hydrolase {ECO:0000313|EMBL:ABV20110.1};
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_5002718857.
FT   DOMAIN      193    637       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   676 AA;  75777 MW;  0736A575A7264431 CRC64;
     MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
     ADAIKLNQML SLQPCSNTPP QWRLFRDGKY TLQIDTRSGT PTLMISIQNA AEPVANLVRE
     CPKWDGLPLT LDVSATFPEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDA
     PAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
     LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGNE ADLRTLVDSA
     HQRGIRILFD VVMNHTGYAT LADMQEYQFG ALYLSGDEVK KTLGERWSDW KPAAGQTWHS
     FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
     YKNKTDTHAK VIEGFTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA
     LREWKKAYPD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
     MDTTWQQMAE KLQGFNVLSY LSSHDTRLFR EGGDKAAELL LLAPGAVQIF YGDESSRPFG
     PTGSDPLQGT RSDMNWQDVS GKSAANVAHW QKISQFRARH PAIGAGKQTT LSLKQGYGFV
     REHGDDKVLV IWAGQQ
//
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