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Database: UniProt
Entry: L9X504_9EURY
LinkDB: L9X504_9EURY
Original site: L9X504_9EURY 
ID   L9X504_9EURY            Unreviewed;      1589 AA.
AC   L9X504;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=C492_15401 {ECO:0000313|EMBL:ELY55673.1};
OS   Natronococcus jeotgali DSM 18795.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=1227498 {ECO:0000313|EMBL:ELY55673.1, ECO:0000313|Proteomes:UP000011531};
RN   [1] {ECO:0000313|EMBL:ELY55673.1, ECO:0000313|Proteomes:UP000011531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18795 {ECO:0000313|EMBL:ELY55673.1,
RC   ECO:0000313|Proteomes:UP000011531};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELY55673.1}.
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DR   EMBL; AOIA01000128; ELY55673.1; -; Genomic_DNA.
DR   STRING; 1227498.C492_15401; -.
DR   PATRIC; fig|1227498.3.peg.3020; -.
DR   OrthoDB; 38162at2157; -.
DR   Proteomes; UP000011531; Unassembled WGS sequence.
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; -; 2.
DR   Gene3D; 2.70.98.10; -; 2.
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; 3.
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; IPR006103; Glyco_hydro_2_cat.
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; 2.
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; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ELY55673.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1081..1570
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   DOMAIN          1230..1358
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1176..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1589 AA;  172558 MW;  30607724DDB10C2C CRC64;
     MSGADEPAET EPVGRRLSTS RRRFLQATGM AALTSGAGVG AAAASDGSSP SRISPGAIDE
     ATLRSYIDDP AVFEENHEPP HVTTTVPFES TEQAVAADVP YERLEDRFDR SPYFRLLDGD
     WRFKRYENYA AVPDSHDDVD WDEIAVPSSW QARGYGQRIY ANTDLTWNHY DPPSDENPVE
     EVPLENNPVG VYRRSFEVPA DWDGRRTHLH FGGVRQAYFV WVDGEYVGYH QGSMTPGEFD
     VTDRVEAGGT HEVTVQVYRF SDGEAVEAQD MFRYSGIFRS VYLYATPRVR VRDFFVRTDL
     DDDYEDATLR VDAELANDGG EPGEYELRGC LYALDSDGPR RGPPEETPGR GPPEDAPGRG
     PRPGDAGDGP SEGPGRGPPG EGSAGREVAT LSGSAAVGAE GAHVSLETAV RDPEKWSAED
     PTLYTLVLEL VPLEGDAPGE VLLEKVGFRA YEAERGALSS AWRVNGEPMN VRGVNRHETD
     PDYGRHVPIE TLRTDFEVMK RFNVNSVRTS HYPNDPSFYR LADEYGIYVQ DEINVETHWW
     EQMAANVDAF DEQILARWRR MVQRDKNHAS VFVYSTGNEA GTGPPHLAMA ADNLGEENAD
     RIPATFEARH LSGADDADRV GEALDLEPRG VDTTRQLYHQ PNGGGWTIDY SDMLGPRYPM
     PDGMVGEGDG SGLGDGERPV MMGEYNHAMG NSLGLIHEMW SEYVQPPVRR ARDGAGENDG
     VLVGSPEVAG DGRVALEGGE YVEVRGAADV ASLETGGTVE VVVRDVDGAT PLVVADGYEL
     SAADGEFEFA VGDASVAASI PDGDGRHTVA GVRADGELRL YVDGELAGVE GDSADGLEFG
     GDLLIGGDPD ADGDVTLESV TLSGAAPDGE GYSSPGEPAL SYDFADLARD KSLQGGWIWD
     WVNQDLNDET DDGEPFQFYH LEGPDGAFCL NGTLWSDRTP QPEMWELKKS HQPVGIAARA
     LEDGELYVTN HFGFTDLSAL ETRWELAADD ETIDSGELDL EIAPGETRPV TVPFEAPDLV
     PGAEYWLDVS VRLAEPTDYA DAGHEVAFEQ FAVPFDVPEP ETERAAAMPG LSVSESDGTI
     AIEGDGFEYA FDSELGTLAS MEYDGTELLE RGPLLNAWRA PIMNEAQDWG GAQAPDWYEA
     GLDDLRHVVE SVEVDRLEDS VARVAVEGFA EGAAVDGGLV TPDASPTGAD GALRGDPEIV
     DGAAGAAVAL DGEDDYLEVG TPDALDFTET GFTVEVTFEG IDDADHGPLL AKGDYQYALK
     TAGGDAFEFF VYDGDWVTLQ APIPETAREG WHTLAGVCDD DELRLYLDGE RLAVEDHAVE
     SVDSSGAPVR IGQNADQDRY VETTVDAAAV YDAALDDETL ADGFDEPPES AVLWYDLDEF
     EEADDEGNGP GFATRYAYRV FGTGEVVLDV ESDPNDRLRS AIGDWLPKVG VRLELPDSFG
     EFEWYGRGPQ ETMPDRKWGV RVGRYSGSVD EQHVPYLPPQ DNGNKAETRW AAVANDDGVG
     LAAVAHPEMH VNLEQYANLD EADHGYELEE RESVGLDLDH AVTGVGGTPT TPLPEYQVRP
     EPMAFTVSLR PFADEDPMAL AKRRLPDAE
//
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