XACK_HALVD
ID XACK_HALVD Reviewed; 383 AA.
AC D4GP39; L9VI55;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Xylose/arabinose import ATP-binding protein XacK {ECO:0000305};
DE EC=7.5.2.13 {ECO:0000269|PubMed:31089701};
GN Name=xacK {ECO:0000303|PubMed:31089701};
GN Synonyms=tsgD7 {ECO:0000312|EMBL:ADE01437.1};
GN OrderedLocusNames=HVO_B0038 {ECO:0000312|EMBL:ADE01437.1};
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;
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 FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INDUCTION.
RC STRAIN=DS2 / DS70 / H26;
RX PubMed=31089701; DOI=10.1093/femsle/fnz089;
RA Johnsen U., Ortjohann M., Sutter J.M., Geweke S., Schoenheit P.;
RT "Uptake of D-xylose and L-arabinose in Haloferax volcanii involves an ABC
RT transporter of the CUT1 subfamily.";
RL FEMS Microbiol. Lett. 366:0-0(2019).
CC -!- FUNCTION: Part of the ABC transporter complex XacGHIJK involved in the
CC uptake of xylose and arabinose (PubMed:31089701). Responsible for
CC energy coupling to the transport system (Probable).
CC {ECO:0000269|PubMed:31089701, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-xylose(out) + H2O = ADP + D-xylose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:29899, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:456216; EC=7.5.2.13;
CC Evidence={ECO:0000269|PubMed:31089701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29900;
CC Evidence={ECO:0000269|PubMed:31089701};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-arabinose(out) = ADP + H(+) + L-arabinose(in) +
CC phosphate; Xref=Rhea:RHEA:30007, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17535, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.5.2.13;
CC Evidence={ECO:0000269|PubMed:31089701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30008;
CC Evidence={ECO:0000269|PubMed:31089701};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (XacJ and
CC XacK), two transmembrane proteins (XacH and XacI) and a solute-binding
CC protein (XacG). {ECO:0000305|PubMed:31089701}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally up-regulated by both L-arabinose and D-
CC xylose via the pentose-specific regulator XacR.
CC {ECO:0000269|PubMed:31089701}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate
CC uptake transporter-1 (CUT1) (TC 3.A.1.1) family. {ECO:0000305}.
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DR EMBL; CP001953; ADE01437.1; -; Genomic_DNA.
DR RefSeq; WP_004041117.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP39; -.
DR SMR; D4GP39; -.
DR STRING; 309800.C498_01570; -.
DR TCDB; 3.A.1.1.56; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE01437; ADE01437; HVO_B0038.
DR GeneID; 8919050; -.
DR KEGG; hvo:HVO_B0038; -.
DR PATRIC; fig|309800.29.peg.299; -.
DR eggNOG; arCOG00177; Archaea.
DR HOGENOM; CLU_000604_1_1_2; -.
DR OMA; RPRNIFV; -.
DR OrthoDB; 88924at2157; -.
DR Proteomes; UP000008243; Plasmid pHV3.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015614; F:ABC-type D-xylose transporter activity; IEA:RHEA.
DR GO; GO:0015612; F:ABC-type L-arabinose transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Plasmid;
KW Reference proteome; Sugar transport; Translocase; Transport.
FT CHAIN 1..383
FT /note="Xylose/arabinose import ATP-binding protein XacK"
FT /id="PRO_0000449390"
FT DOMAIN 4..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 383 AA; 41615 MW; 5E81629F3E9B68CA CRC64;
MARLTLDDVT KVYTDEGGGD IVAVEEISLD IDDGEFLVLV GPSGCGKSTT LRMMAGLETV
TEGELRLEDR VLNGVSAQDR DIAMVFQSYA LYPHKSVRGN MSFGLEESTG LPDDEIRQRV
EETTDMLGIS DLLDRKPGQL SGGQQQRVAL GRAIVRDPEV FLMDEPLSNL DAKLRAEMRT
ELQRLQGELG VTTVYVTHDQ TEAMTMGDRV AVLDDGELQQ VGTPLDCYHR PNNLFVAGFI
GEPSMNLFDG SLSGDTFRGD GFDYPLSGAT RDQLGGASGL TLGIRPEDVT VGERRSGQRT
FDAEVVVVEP QGNENAVHLR FVDGDEGTQF TATTTGQSRV EAGDRTTVSF PEDAIHLFDG
ETGDALKNRE LPSNRAIDAF VSN