RGMG2_BURCM
ID RGMG2_BURCM Reviewed; 524 AA.
AC Q0BG60;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Putative ribose/galactose/methyl galactoside import ATP-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_01717};
DE EC=7.5.2.11 {ECO:0000255|HAMAP-Rule:MF_01717};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01717};
GN OrderedLocusNames=Bamb_1305;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of an ABC transporter complex involved in carbohydrate
CC import. Could be involved in ribose, galactose and/or methyl
CC galactoside import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:60156, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.5.2.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01717};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01717}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01717}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate
CC importer 2 (CUT2) (TC 3.A.1.2) family. {ECO:0000255|HAMAP-
CC Rule:MF_01717}.
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DR EMBL; CP000440; ABI86863.1; -; Genomic_DNA.
DR RefSeq; WP_011656627.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BG60; -.
DR SMR; Q0BG60; -.
DR STRING; 339670.Bamb_1305; -.
DR EnsemblBacteria; ABI86863; ABI86863; Bamb_1305.
DR GeneID; 44691982; -.
DR KEGG; bam:Bamb_1305; -.
DR PATRIC; fig|339670.21.peg.243; -.
DR eggNOG; COG1129; Bacteria.
DR OMA; EGMAVIM; -.
DR Proteomes; UP000000662; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015611; F:ABC-type D-ribose transporter activity; IEA:RHEA.
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; PS51260; MGLA; 1.
DR PROSITE; PS51254; RBSA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Repeat; Sugar transport; Translocase; Transport.
FT CHAIN 1..524
FT /note="Putative ribose/galactose/methyl galactoside import
FT ATP-binding protein 2"
FT /id="PRO_0000277557"
FT DOMAIN 35..271
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT DOMAIN 281..520
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ SEQUENCE 524 AA; 57425 MW; C67CD905F65D4464 CRC64;
MFTARMARPM ANESAPAASF AAPGSSGAPV ADCLLEVRGV GKSFPGVVAL DGVQFRVRRG
TVHALMGENG AGKSTLMKII AGVYTPDQGE ILINGEPVVL SGPLDALDRG IAMIHQELNL
MPYMTVAENI WIRREPKNRF GLIDHAALRR RTAALFERLS IDIDPEADVR TLTVASRQMV
EIAKAVSFDS DVLIMDEPTS ALTDKEVSHL FRIIRQLREQ GKGIVYITHK MNELFEIADE
FSVFRDGKYI GTHASTDVTR DDIIRMMVGR EITQMFPKED VPIGDVVLAV KNLGVDGVFR
DVSFELRAGE ILGVAGLVGS GRSNVAEALF GVVPATAGEI RIDGKPVRIT TPAQAMKHGM
AFLTEDRKDT GCFLNLDLLA NMEAAVLSNR YVKFNFVRQA QLKRDCEAMS RMLRVKTPGL
HEEIQNLSGG NQQKVLIGRW LLTQPRILIL DEPTRGIDVG AKAEIHRLVS ALAGKGVAVL
MISSEMPEVL GMSDRVMVMH EGRMTGIVER KDADQVRIMD LASR