XYLG_SULAC
ID XYLG_SULAC Reviewed; 251 AA.
AC P0DTT6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Xylose/arabinose import ATP-binding protein XylG {ECO:0000305};
DE EC=7.5.2.13 {ECO:0000269|PubMed:29150511};
GN Name=xylG {ECO:0000303|PubMed:29150511};
GN OrderedLocusNames=Saci_2120 {ECO:0000303|PubMed:29150511};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=MW001;
RX PubMed=29150511; DOI=10.1128/aem.01273-17;
RA Wagner M., Shen L., Albersmeier A., van der Kolk N., Kim S., Cha J.,
RA Braesen C., Kalinowski J., Siebers B., Albers S.V.;
RT "Sulfolobus acidocaldarius transports pentoses via a carbohydrate uptake
RT transporter 2 (CUT2)-type ABC transporter and metabolizes them through the
RT aldolase-independent Weimberg pathway.";
RL Appl. Environ. Microbiol. 84:0-0(2018).
CC -!- FUNCTION: Part of the ABC transporter complex XylFGH involved in the
CC uptake of xylose and arabinose (PubMed:29150511). Responsible for
CC energy coupling to the transport system (Probable).
CC {ECO:0000269|PubMed:29150511, 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:29150511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29900;
CC Evidence={ECO:0000269|PubMed:29150511};
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:29150511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30008;
CC Evidence={ECO:0000269|PubMed:29150511};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (XylG),
CC two transmembrane proteins (XylH) and a solute-binding protein (XylF).
CC {ECO:0000305|PubMed:29150511}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated in the presence of D-xylose, L-arabinose and D-
CC arabinose. {ECO:0000269|PubMed:29150511}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in a growth defect
CC on D-xylose and L-arabinose. {ECO:0000269|PubMed:29150511}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; CP000077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_015385776.1; NC_007181.1.
DR AlphaFoldDB; P0DTT6; -.
DR SMR; P0DTT6; -.
DR GeneID; 33346664; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 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;
KW Reference proteome; Sugar transport; Translocase; Transport.
FT CHAIN 1..251
FT /note="Xylose/arabinose import ATP-binding protein XylG"
FT /id="PRO_0000449394"
FT DOMAIN 5..241
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 251 AA; 28014 MW; 2285DD190FEFE473 CRC64;
MSDLLEIRDV HKSFGAVKAL DGVSMEINKG EVVALLGDNG AGKSTLIKII SGYHKPDRGD
LVFEGKKVIF NSPNDARSLG IETIYQDLAL IPDLPIYYNI FLAREVTNKI FLNKKKMMEE
SKKLLDSLQI RIPDINMKVE NLSGGQRQAV AVARAVYFSA KMILMDEPTA ALSVVEARKV
LELARNLKKK GLGVLIITHN IIQGYEVADR IYVLDRGKII FHKKKEETNV EEITEVMTSF
ALGKVNLGEK R
