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Database: UniProt/TrEMBL
Entry: B1LJD3_ECOSM
LinkDB: B1LJD3_ECOSM
Original site: B1LJD3_ECOSM 
ID   B1LJD3_ECOSM            Unreviewed;       676 AA.
AC   B1LJD3;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   SubName: Full=Alpha-amylase, periplasmic {ECO:0000313|EMBL:ACB20009.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ACB20009.1};
GN   Name=malS {ECO:0000313|EMBL:ACB20009.1};
GN   OrderedLocusNames=EcSMS35_3894 {ECO:0000313|EMBL:ACB20009.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB20009.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB20009.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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DR   EMBL; CP000970; ACB20009.1; -; Genomic_DNA.
DR   RefSeq; WP_000761242.1; NC_010498.1.
DR   ProteinModelPortal; B1LJD3; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACB20009; ACB20009; EcSMS35_3894.
DR   KEGG; ecm:EcSMS35_3894; -.
DR   HOGENOM; HOG000273912; -.
DR   KO; K01176; -.
DR   OMA; DKVMVVW; -.
DR   Proteomes; UP000007011; 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:UP000007011};
KW   Glycosidase {ECO:0000313|EMBL:ACB20009.1};
KW   Hydrolase {ECO:0000313|EMBL:ACB20009.1};
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_5002765257.
FT   DOMAIN      193    637       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   676 AA;  75828 MW;  983E7C75509F2623 CRC64;
     MKLAACFLTL LPGFAVAASW TSPGFPAFSE QGTGTFVSHA QLPKGTRPLT LNFDQQCWQP
     ADAIKLNQML SLQPCSNTPP QWRLFRDGEY TLQLDTRSGT PTLMISIQNA VEPVASLVRE
     CPKWDGLPLT LDVSATFPEG AAVRDYYSQQ IAIVKNGQIT LQPAATSNGL LLLERAETDA
     SAPFDWHNAT VYFVLTDRFE NGDPSNDQSY GRHKDGMAEI GTFHGGDLRG LTNKLDYLQQ
     LGVNALWISA PFEQIHGWVG GGTKGDFPHY AYHGYYTQDW TNLDANMGRE ADLRTLVDSA
     HQRGIRILFD VVMNHTGYAT LADMQEFQFG ALYLSGDEVK KTLGERWSDW KPAAGQTWHS
     FNDYINFSDK TGWDKWWGKN WIRTDIGDYD NPGFDDLTMS LAFLPDIKTE STTASGLPVF
     YKNKTDTHAK VIDGFTPRDY LTHWLSQWVR DYGIDGFRVD TAKHVELPAW QQLKTEASAA
     LREWKKANSD KALDDKPFWM TGEAWGHGVM QSDYYRHGFD AMINFDYQEQ AAKAVDCLAQ
     MDTTWQQMAE KLQDFNVLSY LSSHDTRLFR EGGNKAAELL LLAPGAVQIF YGDESSRPFG
     PTGSDPLQGT RSDMNWQDVS GKSAASVAHW QKISQFRARH PAIGEGKQTT LSMKQGYGFV
     REHGDDKVLV IWAGQQ
//
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