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Database: UniProt
Entry: Q2YYJ9
LinkDB: Q2YYJ9
Original site: Q2YYJ9 
ID   LACG_STAAB              Reviewed;         470 AA.
AC   Q2YYJ9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   14-MAY-2014, entry version 66.
DE   RecName: Full=6-phospho-beta-galactosidase;
DE            EC=3.2.1.85;
DE   AltName: Full=Beta-D-phosphogalactoside galactohydrolase;
DE            Short=PGALase;
DE   AltName: Full=P-beta-Gal;
DE            Short=PBG;
GN   Name=lacG; OrderedLocusNames=SAB2070c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- CATALYTIC ACTIVITY: A 6-phospho-beta-D-galactoside + H(2)O = 6-
CC       phospho-D-galactose + an alcohol.
CC   -!- PATHWAY: Carbohydrate metabolism; lactose degradation; D-galactose
CC       6-phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
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DR   EMBL; AJ938182; CAI81759.1; -; Genomic_DNA.
DR   RefSeq; YP_417528.1; NC_007622.1.
DR   ProteinModelPortal; Q2YYJ9; -.
DR   SMR; Q2YYJ9; 1-470.
DR   STRING; 273036.SAB2070c; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   EnsemblBacteria; CAI81759; CAI81759; SAB2070c.
DR   GeneID; 3794800; -.
DR   KEGG; sab:SAB2070c; -.
DR   PATRIC; 19525167; VBIStaAur92441_2179.
DR   eggNOG; COG2723; -.
DR   HOGENOM; HOG000088632; -.
DR   KO; K01220; -.
DR   OMA; ANESIPR; -.
DR   OrthoDB; EOG60658J; -.
DR   BioCyc; SAUR273036:GJVS-2144-MONOMER; -.
DR   UniPathway; UPA00542; UER00605.
DR   GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:InterPro.
DR   Gene3D; 3.20.20.80; -; 1.
DR   HAMAP; MF_01574; LacG; 1.
DR   InterPro; IPR005928; 6P-beta-galactosidase.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR01233; lacG; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycosidase; Hydrolase.
FT   CHAIN         1    470       6-phospho-beta-galactosidase.
FT                                /FTId=PRO_0000260724.
FT   ACT_SITE    160    160       Proton donor (By similarity).
FT   ACT_SITE    375    375       Nucleophile (By similarity).
SQ   SEQUENCE   470 AA;  54565 MW;  9A5C8E295AB8DF2F CRC64;
     MTKTLPEDFI FGGATAAYQA EGATNTDGKG RVAWDTYLEE NYWYTAEPAS DFYNRYPVDL
     ELSEKFGVNG IRISIAWSRI FPNGYGEVNP KGVEYYHKLF AECHKRHVEP FVTLHHFDTP
     EVLHKDGDFL NRKTIDYFVD YAEYCFKEFP EVKYWTTFNE IGPIGDGQYL VGKFPPGIKY
     DFEKVFQSHH NMMVAHARAV KLFKDGGYQG EIGVVHALPT KYPFDPSNPE DVRAAELEDI
     IHNKFILDAT YLGKYSRETM EGVQHILSVN GGKLNITDED YAILDAAKDL NDFLGINYYM
     SDWMRGYDGE SEITHNATGD KGGSKYQLKG VGQREFDVDV PRTDWDWMIY PQGLYDQIMR
     VVKDYPNYHK IYITENGLGY KDEFIESEKT VHDDARIDYV RQHLNVIADA IKDGANVKGY
     FIWSLMDVFS WSNGYEKRYG LFYVDFETQE RYPKKSAYWY KELAETKEIK
//
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