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Database: UniProt
Entry: B7R523_9EURY
LinkDB: B7R523_9EURY
Original site: B7R523_9EURY 
ID   B7R523_9EURY            Unreviewed;       444 AA.
AC   B7R523;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Beta-galactosidase trimerisation domain-containing protein {ECO:0000259|Pfam:PF08532};
GN   ORFNames=TAM4_2051 {ECO:0000313|EMBL:EEB73194.1};
OS   Thermococcus sp. AM4.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB73194.1, ECO:0000313|Proteomes:UP000009277};
RN   [1] {ECO:0000313|EMBL:EEB73194.1, ECO:0000313|Proteomes:UP000009277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM4 {ECO:0000313|EMBL:EEB73194.1,
RC   ECO:0000313|Proteomes:UP000009277};
RX   PubMed=22123768; DOI=10.1128/JB.06259-11;
RA   Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H.,
RA   Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
RT   "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus
RT   sp. Strain AM4, Capable of Organotrophic Growth and Growth at the Expense
RT   of Hydrogenogenic or Sulfidogenic Oxidation of Carbon Monoxide.";
RL   J. Bacteriol. 193:7019-7020(2011).
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DR   EMBL; CP002952; EEB73194.1; -; Genomic_DNA.
DR   RefSeq; WP_014121694.1; NC_016051.1.
DR   AlphaFoldDB; B7R523; -.
DR   STRING; 246969.TAM4_2051; -.
DR   GeneID; 7419143; -.
DR   KEGG; tha:TAM4_2051; -.
DR   eggNOG; arCOG02611; Archaea.
DR   HOGENOM; CLU_614854_0_0_2; -.
DR   OrthoDB; 101158at2157; -.
DR   Proteomes; UP000009277; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        260..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..209
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
SQ   SEQUENCE   444 AA;  50069 MW;  FDF0787EBB19A91D CRC64;
     MTRLGSKLLV VFLFFALLFH LPPNYASPNE KARILVVCSD PEDVMFANTL GAEGNFTVDV
     LYLGRDLPDD RSLLSNELYL IKYDEIWIPD LNAGLTEGGR LNREETSALA EYVRRGGVLV
     LGLNTYTQSW SRTLERITGT RLMRIEKPEE ASDEWNLVFE GRVYPYNATY QVAVVTPYRA
     QVLARYSNGL PAVTLSRYGR GVGVLMTFNP VKELVEYNPE IIDVYVHVAN IALSERSGKP
     EIPAGEAVLL KLERVLLHPV FLGVLVFVLL EIMAYLGFLP FSVTVLFAVP LLPFSRFLLG
     RAPYSAILEI VRMLRGVTLG NLADEIGRSP RRLKFPLALL FLKKQISVID LSPFGFKDVL
     VVLRGLEGDG VAAWAIEVYP RMMEIIASNP GIGVIDLARQ VNMPPYDVLR LLRELSRYGV
     VELRKIVVDY EVYPMRPLLR WFEV
//
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