ID B7MD17_ECO45 Unreviewed; 1024 AA.
AC B7MD17;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
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; DFHVATH; -.
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:EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF74650; Gal_mut_like; 1.
DR SUPFAM; SSF49303; Glyco_hydro_2Ig; 2.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 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
//
