XACG_HALVD
ID XACG_HALVD Reviewed; 459 AA.
AC D4GP35;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Xylose/arabinose-binding protein XacG {ECO:0000305};
GN Name=xacG {ECO:0000303|PubMed:31089701};
GN Synonyms=tsgA7 {ECO:0000312|EMBL:ADE01390.1};
GN OrderedLocusNames=HVO_B0034 {ECO:0000312|EMBL:ADE01390.1};
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, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
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. {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}; Single-pass membrane
CC protein {ECO:0000255}; Extracellular side
CC {ECO:0000305|PubMed:31089701}.
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 -!- DISRUPTION PHENOTYPE: Deletion mutant shows decreased growth rate on
CC arabinose or xylose. It cannot grow on low concentrations of arabinose
CC or xylose. {ECO:0000269|PubMed:31089701}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; CP001953; ADE01390.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GP35; -.
DR SMR; D4GP35; -.
DR STRING; 309800.C498_01590; -.
DR TCDB; 3.A.1.1.56; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE01390; ADE01390; HVO_B0034.
DR KEGG; hvo:HVO_B0034; -.
DR eggNOG; arCOG00150; Archaea.
DR HOGENOM; CLU_031285_15_1_2; -.
DR OMA; GKDYGCM; -.
DR Proteomes; UP000008243; Plasmid pHV3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR006059; SBP.
DR Pfam; PF13416; SBP_bac_8; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Plasmid; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..459
FT /note="Xylose/arabinose-binding protein XacG"
FT /id="PRO_0000449393"
FT TRANSMEM 19..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 27..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 49253 MW; B0A57D2428A22C6B CRC64;
MVEHDSSDES VNRRKYLKAL TVGAAAGIAG CTGGGGTETE STESGNGNGS GGSTDDTETS
GSSSGESWDS QLEVLHGWAG GDGEAAVTAL IEAFEEEHPE MDTNFQAVGA SANVNLNATI
LRRLANNNPM SSFANWPGKN LERYSGALMD LEADVWDAEG FKDTMQSRAV ELCKFNDKMP
AVPIGSHRMN NLFYNTAVFE EAGIDASSLD SVDALLDALE TIDQNTDVTP MAQAMVAPWT
NLQLWAQILT SQSGVEAYTN FIEGNPDRAA VVEALEALKT INENYITADA SSISFTTAGQ
KVISGKAATI HQGNWVYGMF RADDSFNYKE QWDWIPFPGT EGIYFYHVDS IVAPSNNPSR
EETIAWQKFV GSKKAQIAFN NPKGSVPLRT DIDPSELTDF LAMTYEDLTD SEAYPPTIAH
GLAVTPKTMG ACKTAFGDNF MGPFNVEATA DALVAAVSE