ARAG_RHIME
ID ARAG_RHIME Reviewed; 508 AA.
AC Q92W56;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Arabinose import ATP-binding protein AraG {ECO:0000255|HAMAP-Rule:MF_01721};
DE EC=7.5.2.12 {ECO:0000255|HAMAP-Rule:MF_01721};
GN Name=araG {ECO:0000255|HAMAP-Rule:MF_01721}; OrderedLocusNames=RB0489;
GN ORFNames=SMb20507;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Part of the ABC transporter complex AraFGH involved in
CC arabinose import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01721}.
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=7.5.2.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01721};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (AraG),
CC two transmembrane proteins (AraH) and a solute-binding protein (AraF).
CC {ECO:0000255|HAMAP-Rule:MF_01721}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01721}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01721}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Arabinose
CC importer (TC 3.A.1.2.2) family. {ECO:0000255|HAMAP-Rule:MF_01721}.
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DR EMBL; AL591985; CAC48889.1; -; Genomic_DNA.
DR PIR; A95903; A95903.
DR RefSeq; NP_437029.1; NC_003078.1.
DR RefSeq; WP_010975368.1; NC_003078.1.
DR AlphaFoldDB; Q92W56; -.
DR SMR; Q92W56; -.
DR STRING; 266834.SM_b20507; -.
DR PRIDE; Q92W56; -.
DR DNASU; 1236820; -.
DR EnsemblBacteria; CAC48889; CAC48889; SM_b20507.
DR GeneID; 61600498; -.
DR KEGG; sme:SM_b20507; -.
DR PATRIC; fig|266834.11.peg.5421; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_5; -.
DR OMA; NVHLGHE; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 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.
DR PROSITE; PS51268; ARAG; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Plasmid; Reference proteome; Repeat; Sugar transport;
KW Translocase; Transport.
FT CHAIN 1..508
FT /note="Arabinose import ATP-binding protein AraG"
FT /id="PRO_0000270477"
FT DOMAIN 5..240
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT DOMAIN 250..496
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ SEQUENCE 508 AA; 55515 MW; 6282826D5128130E CRC64;
MQDFLEFQSI SKGYPGVQAL SEVSFSVRKG AVHGLMGENG AGKSTLIRVL SGDQAADTGE
IRINGEPQHY RSVRDAFNAG VIVIHQELQL VPELTVAENL WLGRFPGKAG VIDRRQLIRV
VSDRLAEIGI DVDPEAKVAS LSIGERQMVE IAKAVMTDAR VIALDEPTSS LSSRESEILF
ALIDRLRSNG TVILYVSHRL DEIFRLCNSL TVLRDGRLAA HHPDISKVGR EQIIAEMVGR
EISNIWGWRA RTLGAARLTV ERVSGANLPQ PISFTVRAGE ILGFFGLIGA GRSEMARLVY
GADRRRQGKV LVDGLAVPAD SPRLSIRAGV VLCPEDRKFD GIVQGRSIEE NMAISSRRHF
SPFGVVDKGK EAELAERFIA KLRVRTPSRH QDIVNLSGGN QQKVILGRWL SEEGVKVLLI
DEPTRGIDVG AKSEIYEILY ELAAQGMAIV VISSELPEVM GIADRILVMC EGRIAAEIDR
SDFDEHRILA AALPDASATT ATLPEQVS
