ID   BGAM_LACHE              Reviewed;         318 AA.
AC   Q7WTB3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Beta-galactosidase small subunit {ECO:0000305|PubMed:12788721};
DE            Short=Beta-gal small subunit {ECO:0000305|PubMed:12788721};
DE            EC=3.2.1.23 {ECO:0000250|UniProtKB:Q02604};
GN   Name=lacM {ECO:0000303|PubMed:12788721};
OS   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=ATCC 15009 / DSM 20075 / BCRC 12936 / JCM 1120 / NBRC 15019 /
RC   NCIMB 11971 / NRRL B-4526 / Lh12;
RX   PubMed=12788721; DOI=10.1128/aem.69.6.3238-3243.2003;
RA   Fortina M.G., Ricci G., Mora D., Guglielmetti S., Manachini P.L.;
RT   "Unusual organization for lactose and galactose gene clusters in
RT   Lactobacillus helveticus.";
RL   Appl. Environ. Microbiol. 69:3238-3243(2003).
CC   -!- FUNCTION: Component of a beta-galactosidase.
CC       {ECO:0000250|UniProtKB:Q02604}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000250|UniProtKB:Q02604};
CC   -!- SUBUNIT: Heterodimer of a large (LacL) and a small subunit (LacM).
CC       {ECO:0000250|UniProtKB:Q02604}.
CC   -!- INDUCTION: By lactose. Part of an operon consisting of lacL, lacM, and
CC       galE. {ECO:0000269|PubMed:12788721}.
CC   -!- SIMILARITY: Belongs to the bacterial beta-galactosidase small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AJ512877; CAD55500.1; -; Genomic_DNA.
DR   RefSeq; WP_003627057.1; NZ_SCLV01000128.1.
DR   AlphaFoldDB; Q7WTB3; -.
DR   SMR; Q7WTB3; -.
DR   eggNOG; COG3250; Bacteria.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..318
FT                   /note="Beta-galactosidase small subunit"
FT                   /id="PRO_0000057668"
SQ   SEQUENCE   318 AA;  35895 MW;  0BDB79B71E6D58C1 CRC64;
     MDYTNNQLHI IYGDATLGVN GKDFQYIFSY ERGGLESLKV HGKEWLYRVP TPTFWRATTD
     NDRGSGFNLK AAQWLGADMF TKCTDIHLKV DRHDFAELPI APFNNKFSNH EYAKSAEISF
     TYQTLTTPAT NAKIIYNIDD VGHIKVTMRY YGKKGLPPLP VIGIRLIMPT AATGFDYEGL
     SGETYPDRMA GAKEGKFHID GLPVTEYLVP QENGMHMQTK KLTINRETTQ NNVDRTNEKF
     SLSIQQAEKP FNFSCLPYTA EELENATHIE ELPLVRRTVL VIAGAVRGVG GIDSWGTDVE
     SAYHINPELD HEFSFILN
//