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RBSA2_RHIEC
ID   RBSA2_RHIEC             Reviewed;         508 AA.
AC   Q2K204;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Ribose import ATP-binding protein RbsA 2 {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA2 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   OrderedLocusNames=RHE_PB00077;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42b.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC       import. Responsible for energy coupling to the transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_01716}.
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_01716};
CC   -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), two
CC       transmembrane proteins (RbsC) and a solute-binding protein (RbsB).
CC       {ECO:0000255|HAMAP-Rule:MF_01716}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01716}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01716}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer
CC       (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}.
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DR   EMBL; CP000135; ABC93119.1; -; Genomic_DNA.
DR   RefSeq; WP_011427541.1; NC_007763.1.
DR   AlphaFoldDB; Q2K204; -.
DR   SMR; Q2K204; -.
DR   EnsemblBacteria; ABC93119; ABC93119; RHE_PB00077.
DR   KEGG; ret:RHE_PB00077; -.
DR   HOGENOM; CLU_000604_92_2_5; -.
DR   OMA; IDWKEMR; -.
DR   Proteomes; UP000001936; Plasmid p42b.
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; PS51254; RBSA; 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="Ribose import ATP-binding protein RbsA 2"
FT                   /id="PRO_0000261081"
FT   DOMAIN          6..241
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          254..499
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   508 AA;  54514 MW;  09BC1A8126C6B54B CRC64;
     MAEPVLTIHG VTKHFGAVKA LRDVDFTLER GEVHALCGEN GAGKSTLMNI IAGVLQPTEG
     EIRVDGKAVR ISSPAAAQYL GIGLVHQEIA LCPDATVAEN MFMAATNRRR APLMNYRRLE
     RDAQAVMNRL AAIDVRRRVA DLPISSQQLV EIAKALTLDC RVLILDEPTA ALTETEAQQL
     FSIIRDLKAN GISIIYISHR MAEIFSLCDR VTVFRDGRYV CTDRLADLTP DDVVRRMVGR
     EITQLYPDKL GADERSGGII LEVDGISDGA RFHDVTFGLR KGEILGIGGL IGSGRTEIAE
     GICGLRPRTA GTVRLHGAAQ PIRAYSDAVK AGIVYLSEDR KGSGIFLEMS IAQNISVLDL
     KALTNAVGLL NGRAEAALAD DFARRLAVRM SGIEAPVKSL SGGNQQKVAI AKQLAVKPKV
     ILMDEPTRGI DVGAKAEIHR VLRELASAGI GIIVISSEMP ELLGLSDRLL VVREGRIAGE
     LSADEMSEEA VIRLASGMGS ARAADHAA
 
 
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