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Database: UniProt/TrEMBL
Entry: B7MD17_ECO45
LinkDB: B7MD17_ECO45
Original site: B7MD17_ECO45 
ID   B7MD17_ECO45            Unreviewed;      1024 AA.
AC   B7MD17;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   19-FEB-2014, entry version 38.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=ECS88_0351;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
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).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- COFACTOR: Binds 1 sodium ion per monomer (By similarity).
CC   -!- COFACTOR: Binds 2 magnesium ions per monomer (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
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DR   EMBL; CU928161; CAR01702.1; -; Genomic_DNA.
DR   RefSeq; YP_002390181.1; NC_011742.1.
DR   ProteinModelPortal; B7MD17; -.
DR   SMR; B7MD17; 14-1024.
DR   STRING; 585035.ECS88_0351; -.
DR   EnsemblBacteria; CAR01702; CAR01702; ECS88_0351.
DR   GeneID; 7130472; -.
DR   KEGG; ecz:ECS88_0351; -.
DR   PATRIC; 18408368; VBIEscCol91599_0346.
DR   eggNOG; COG3250; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; HRCAWDQ; -.
DR   OrthoDB; EOG6XWV0T; -.
DR   ProtClustDB; PRK09525; -.
DR   BioCyc; ECOL585035:GJWP-347-MONOMER; -.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.320; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.80; -; 1.
DR   HAMAP; MF_01687; Beta_gal; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR006103; Glyco_hydro_2_TIM.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycosidase; Hydrolase; Magnesium; Metal-binding;
KW   Sodium.
FT   REGION      538    541       Substrate binding (By similarity).
FT   ACT_SITE    462    462       Proton donor (By similarity).
FT   ACT_SITE    538    538       Nucleophile (By similarity).
FT   METAL       202    202       Sodium (By similarity).
FT   METAL       417    417       Magnesium 1 (By similarity).
FT   METAL       419    419       Magnesium 1 (By similarity).
FT   METAL       462    462       Magnesium 1 (By similarity).
FT   METAL       598    598       Magnesium 2 (By similarity).
FT   METAL       602    602       Sodium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       605    605       Sodium (By similarity).
FT   BINDING     103    103       Substrate (By similarity).
FT   BINDING     202    202       Substrate (By similarity).
FT   BINDING     462    462       Substrate (By similarity).
FT   BINDING     605    605       Substrate (By similarity).
FT   BINDING    1000   1000       Substrate (By similarity).
FT   SITE        358    358       Transition state stabilizer (By
FT                                similarity).
FT   SITE        392    392       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   1024 AA;  116503 MW;  BFC6CD845D16A806 CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPAENP
     TGCYSLTFNI DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLHA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFQVTT RFNDDFSRAV
     LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPE
     LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN EFLHWMVALD
     GKPLASGEVP LDVGPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPSASHAIPQ LTTSGTDFCI ELGNKRWQFN RQSGFLSQMW IGDEKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GHGEMVINVD VAVASDTPHP ARIGLTCQLA QVSERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//
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