ID C9Z789_STRSW Unreviewed; 1311 AA.
AC C9Z789;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN OrderedLocusNames=SCAB_44201 {ECO:0000313|EMBL:CBG71483.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG71483.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG71483.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG71483.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; FN554889; CBG71483.1; -; Genomic_DNA.
DR RefSeq; WP_013002093.1; NC_013929.1.
DR STRING; 680198.SCAB_44201; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 24306439; -.
DR KEGG; scb:SCAB_44201; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_2_1_11; -.
DR Proteomes; UP000001444; Chromosome.
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 GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 2.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 672..803
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 1018..1292
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1311 AA; 144749 MW; A6FAF1E611486306 CRC64;
MPHPHPHTGT PAARPVMSRR RLLEGGAALL GAVALSGGAA HAAPLLASKA DGTPEWSGNM
ALFQVGAEPP HTTLMPYADV RQALAADRTR SPYRLSLDGK WRFAYVERPG DRDEDFYKTD
VDDSDWDTIP VPSNWQLHGY DFPIYINITY PWWGPNGLGE EAQPPNAPTR YNPVGQYRRS
FNLPKDWTAG DRRTFLHFEG VKSAHYVWIN GELVGYHEDS YDPAEYDITP HLKPGSNQIA
VEVYRYSDGD WLEDQDMIRL SGIFRSVYLY STPAVHLRDF KLDTPLGDGY TTAELSVTAS
VRAYAAGHEG AYSVETQLYD AGGHAVWSRP LVQSVTVGAS ATGEDVTVQA ARSVPSPELW
SAEHPTLYTA VLQLRDPAGK VVETLSHRVG LREFALRNGL MRINGKPVSL RGTNRHEMHP
DRGMALTRAD LVQDMGIIKR LNINSVRTSH YPNNPLWYEL ADEYGLYLVD ETNLETHGIR
DRFPGNDPDW TKACVARARN MVHRDKNHAS VVIWSLGNEA GGGSTFVAMR DWIESYDKTR
VIQYEGDDRP TISQIRSEMY DSPQRVEQRA KDTSDTRPYV MIEYSHSMGN STGNFKKYWD
LVRRYPVLQG GWIWDFVDQS LTWPIPRLKV FTDAGPSKLQ GQLLTAAGTF SRDKGLSGAT
GFTRDPALNL TGSLTLEAWF TPHVTGGHQP IIAKGDTHYA LKQSEKSIEF FIYGGGQWVS
VSWGLPAEGW TGREHHVAGV FDAGSGSLTL YVDGEVKATR STTRRPSANV APLALGTDTD
NPTRELSGTI RRARVYARAL SGSELASTGR GAGDEGVRFW FDAATVEVKE SRAKDRSFLA
YGGDWGDNPN DGAFVADGII KADRGHTGKA AEVKRIYQAV HAKPATGTTL ASKKVTLTNE
FLFTNLRELD GGWTLVADGR KIQEGRLTRD QLDVGPLSAK DITVPFDLPA SPAPGTEYFL
ELSFTTKDSA PWAEAGFEVA REQLSVDAGS PAVTPVPLAD VPELTYEESD EAVTVTGKGY
PGRFSVTVDK ASGTITSYKA GGNRLISDGP VPNFWRAPTD NDHGNGQHTR NQTWRDAGTN
RKVTSVTVRS LGDDRAVEIK VTGTLPTTTE STYTTTYTVF GNAEIKVDNT LHPGASSLPY
IPEVGTLFLL NRRLERLHYY GRGPEENHWD RNNGTDVGLY SGDIADQWSG YIRPQENGNK
TDVRWAAVTD RNGEGLLVSG DGLIEINASY FTPEDLSTGL RHDYHLTPRD TPVLRVNHRQ
MGVGGDNSWG AHTHDEYKLF ANRDYTYTYR LRPLTDVAGA TAASRRPTAT R
//
