ID   LACG2_STRR6             Reviewed;         468 AA.
AC   Q8DPP6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=6-phospho-beta-galactosidase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01574};
DE            Short=PGALase 2 {ECO:0000255|HAMAP-Rule:MF_01574};
DE   AltName: Full=P-beta-Gal 2 {ECO:0000255|HAMAP-Rule:MF_01574};
DE            Short=PBG 2 {ECO:0000255|HAMAP-Rule:MF_01574};
GN   Name=lacG2 {ECO:0000255|HAMAP-Rule:MF_01574}; OrderedLocusNames=spr1069;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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}.
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DR   EMBL; AE007317; AAK99872.1; -; Genomic_DNA.
DR   PIR; D98005; D98005.
DR   RefSeq; NP_358662.1; NC_003098.1.
DR   RefSeq; WP_000169251.1; NC_003098.1.
DR   AlphaFoldDB; Q8DPP6; -.
DR   SMR; Q8DPP6; -.
DR   STRING; 171101.spr1069; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   EnsemblBacteria; AAK99872; AAK99872; spr1069.
DR   GeneID; 60233578; -.
DR   KEGG; spr:spr1069; -.
DR   PATRIC; fig|171101.6.peg.1161; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_9; -.
DR   OMA; RIDYFSH; -.
DR   UniPathway; UPA00542; UER00605.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033920; F:6-phospho-beta-galactosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
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 2"
FT                   /id="PRO_0000260733"
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"
SQ   SEQUENCE   468 AA;  53927 MW;  075F73A048259D7A CRC64;
     MTKTLPKDFI FGGATAAYQA EGATHTDGKG PVAWDKYLED NYWYTAEPAS DFYNRYPVDL
     KLAEEYGVNG IRISIAWSRI FPTGYGQVNA KGVEFYHNLF AECHKRHVEP FVTLHHFDTP
     EALHSNGDFL NRENIEHFVD YAAFCFEEFP EVNYWTTFNE IGPIGDGQYL VGKFPPGIQY
     DLAKVFQSHH NMMVSHARAV KLYKDKGYKG EIGVVHALPT KYPLDHENPA DVRAAELEDI
     IHNKFILDAT YLGRYSAETM EGVNHILSVN GGSLDLREED FTALEAAKDL NDFLGINYYM
     SDWMEAFDGE TEIIHNGKGK KGSSKYQIKG VGRRVAPDYV PRTDWDWIIY PQGLYDQIMR
     VKKDYPNYKK IYITENGLGY KDEFVDNTVY DDGRIDYVKQ HLEILSDAIA DGANVKGYFI
     WSLMDVFSWS NGYEKRYGLF YVDFETQERY PKKSAHWYKK VAETQIID