ID   LACG_STRGC              Reviewed;         468 AA.
AC   Q9EV38; A8AYD1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=6-phospho-beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01574};
DE            EC=3.2.1.85 {ECO:0000255|HAMAP-Rule:MF_01574};
DE   AltName: Full=Beta-D-phosphogalactoside galactohydrolase {ECO:0000255|HAMAP-Rule:MF_01574};
DE            Short=PGALase {ECO:0000255|HAMAP-Rule:MF_01574};
DE   AltName: Full=P-beta-Gal {ECO:0000255|HAMAP-Rule:MF_01574};
DE            Short=PBG {ECO:0000255|HAMAP-Rule:MF_01574};
GN   Name=lacG {ECO:0000255|HAMAP-Rule:MF_01574}; OrderedLocusNames=SGO_1512;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bolken T.C., Franke C.A., Hruby D.E., Zeller G.O.;
RT   "Identification of new intergenic and intragenic integration sites for
RT   foreign gene expression in recombinant Streptococcus gordonii strains.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-phospho-beta-D-galactoside + H2O = an alcohol + D-
CC         galactose 6-phosphate; Xref=Rhea:RHEA:24568, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:58534, ChEBI:CHEBI:91004; EC=3.2.1.85;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01574};
CC   -!- PATHWAY: Carbohydrate metabolism; lactose degradation; D-galactose 6-
CC       phosphate and beta-D-glucose from lactose 6-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01574}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01574}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF210773; AAG39001.1; -; Genomic_DNA.
DR   EMBL; CP000725; ABV10357.1; -; Genomic_DNA.
DR   RefSeq; WP_012130586.1; NC_009785.1.
DR   AlphaFoldDB; Q9EV38; -.
DR   SMR; Q9EV38; -.
DR   STRING; 467705.SGO_1512; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   EnsemblBacteria; ABV10357; ABV10357; SGO_1512.
DR   KEGG; sgo:SGO_1512; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_9; -.
DR   OMA; DWVYVVP; -.
DR   UniPathway; UPA00542; UER00605.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:InterPro.
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; IPR033132; Glyco_hydro_1_N_CS.
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   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..468
FT                   /note="6-phospho-beta-galactosidase"
FT                   /id="PRO_0000260729"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01574"
FT   CONFLICT        459..460
FT                   /note="RR -> KK (in Ref. 1; AAG39001)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   468 AA;  54111 MW;  86A4A0301682873E CRC64;
     MTKSLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYHKYPVDL
     KLAEEYGVNG IRISIAWSRI FPTGYGEVNP KGVEFYHNLF AECHKRHVEP FVTLHHFDTP
     EALHSNGDFL NRDNIEHFVD YAAFCFEEFP EVRYWTTFNE IGPIGDGQYL VGKFPPGIQY
     DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPYDPENPA DVRAAELEDI
     IHNKFILDAT YLGHYSDVTL AGVNHILKVN GGQLDLRDED FAALEAAKDL NDFLGINYYM
     SDWMRDFDGE TEIIHNGKGE KGSSKYQIKG VGRRESPTHI PKTDWDWIIY PQGLYDQIMR
     IKKDYPNYKK IYITENGLGY KDEFVDNTVY DDARIDYVKQ HLEVLSDAIA DGANVKGYFI
     WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAHWYRR LAETQMIE