XACJ_HALVD
ID XACJ_HALVD Reviewed; 383 AA.
AC D4GP38; L9VHW3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Xylose/arabinose import ATP-binding protein XacJ {ECO:0000305};
DE EC=7.5.2.13 {ECO:0000269|PubMed:31089701};
GN Name=xacJ {ECO:0000303|PubMed:31089701};
GN Synonyms=tsgE7 {ECO:0000312|EMBL:ADE01308.1};
GN OrderedLocusNames=HVO_B0037 {ECO:0000312|EMBL:ADE01308.1};
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; ADE01308.1; -; Genomic_DNA.
DR RefSeq; WP_004041118.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP38; -.
DR SMR; D4GP38; -.
DR STRING; 309800.C498_01575; -.
DR TCDB; 3.A.1.1.56; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE01308; ADE01308; HVO_B0037.
DR GeneID; 8919354; -.
DR KEGG; hvo:HVO_B0037; -.
DR PATRIC; fig|309800.29.peg.300; -.
DR eggNOG; arCOG00177; Archaea.
DR HOGENOM; CLU_000604_1_1_2; -.
DR OMA; TETYVYG; -.
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 XacJ"
FT /id="PRO_0000449389"
FT DOMAIN 4..235
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 383 AA; 42764 MW; D2E5C347BE63B98F CRC64;
MGQIQLTDLT KRFGDTVAVD DLSLDIDDEE FLVLVGPSGC GKSTTLRMLA GLETPTSGDI
YIGGDHMNYR VPQNRDIAMV FQDYALYPHM TVRQNIRFGL EEEEGYTSAE RDERVVEVAE
TLGIADLLDR KPDELSGGQQ QRVALGRAIV RDPEVFLMDE PLSNLDAKLR AEMRTELQNL
QDQLAVTTVY VTHNQTEAMT MADRIAVMDD GELQQVASPF ECYHEPNNLF VAEFIGEPMI
NLVRGTRSES TFVGEHFSYP LDEDVMESVD DRDDFVLGVR PEDIEVADAA PDDAALDDHD
LQMDVTVVEP HGDQNVLHLS HPDQPSADDA LQAVTEGMHL VTRGDRVTVT IPPDKIHLFD
AETGTAVHNR RHDQEADFTQ LEQ
