ID   TSGDD_HALVD             Reviewed;         550 AA.
AC   D4GPW3; Q9Y8J8;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Glucose import ATP-binding protein TsgD13;
DE            EC=7.5.2.- {ECO:0000305|PubMed:10430572};
GN   Name=tsgD13; OrderedLocusNames=HVO_B0316;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV3.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2; PLASMID=pHV3;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-550, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=DS2 / WR 340;
RX   PubMed=10430572; DOI=10.1093/genetics/152.4.1417;
RA   Wanner C., Soppa J.;
RT   "Genetic identification of three ABC transporters as essential elements for
RT   nitrate respiration in Haloferax volcanii.";
RL   Genetics 152:1417-1428(1999).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in glucose import
CC       (Probable). Responsible for energy coupling to the transport system (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:10430572, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose(out) + H2O = ADP + D-glucose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:60184, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:10430572};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60185;
CC         Evidence={ECO:0000305|PubMed:10430572};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TsgD13),
CC       two transmembrane proteins (TsgB13 and TsgC13) and a solute-binding
CC       protein (TsgA13). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutant with a disruption within tsgB13 or tsgD13
CC       cannot use glucose for nitrate respirative growth. However, the mutant
CC       can grow aerobically using glucose as the sole energy source.
CC       {ECO:0000269|PubMed:10430572}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CP001953; ADE01548.1; -; Genomic_DNA.
DR   EMBL; AJ238879; CAB42544.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GPW3; -.
DR   SMR; D4GPW3; -.
DR   STRING; 309800.C498_02085; -.
DR   PRIDE; D4GPW3; -.
DR   EnsemblBacteria; ADE01548; ADE01548; HVO_B0316.
DR   KEGG; hvo:HVO_B0316; -.
DR   eggNOG; arCOG00186; Archaea.
DR   HOGENOM; CLU_000604_92_0_2; -.
DR   OMA; IKMLSGA; -.
DR   Proteomes; UP000008243; Plasmid pHV3.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Plasmid;
KW   Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..550
FT                   /note="Glucose import ATP-binding protein TsgD13"
FT                   /id="PRO_0000420944"
FT   DOMAIN          7..270
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          287..533
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          529..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   550 AA;  59405 MW;  74D732A31E3A1858 CRC64;
     MTREPFLRME NIVKAFPGVV ANDHIDLTVE RGEIHGLLGE NGAGKSTLMK ILYGLYSQDD
     GEISLSGTRL RLDSPQDAID AGIGMVHQHF MLIPRLTVAE NVVLGEREPA TPFRPDADAG
     GWLPDAVRSN SLVQSLAGRF SLGLDVPERR IQELADRYGF DIDVSAKVWE LGVGQQQRVE
     ILKALYRDVD LLILDEPTAV LTPTEADLLF DSLERLTDEG VSIIFITHKL EEVEAVVDRV
     TVLRDGENVG TVSTSDVSRA DLAEMMVGRE VLFTVDRERV APGEPVLRAR NVSATDDRGI
     EALSNVDLTV RRGEVVGIAG VSGNGQKELA EVIAGLRTVS AGELTVDGRD LTNASPRTFI
     DNGVSFVPED RNRYGSAGDL SVMHNAAMKD FREDRFGSGV TLDYGELRAH AEALVEAFDV
     RGVHDVTDAT AGDLSGGNLQ KLILAREISR DPDLLVANQP TRGVDVGAIE SIREAILDQR
     TEGTGVVLLS EDLDEIIDLS DRILVVYEGE VVYETTPEDA DRERIGLEMT GGGDATATAG
     AQVRGLGGSS