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RBSA1_BURTA
ID   RBSA1_BURTA             Reviewed;         506 AA.
AC   Q2SVU4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ribose import ATP-binding protein RbsA 1 {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA1 {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=BTH_I2434;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC39265.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000086; ABC39265.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2SVU4; -.
DR   SMR; Q2SVU4; -.
DR   PRIDE; Q2SVU4; -.
DR   EnsemblBacteria; ABC39265; ABC39265; BTH_I2434.
DR   KEGG; bte:BTH_I2434; -.
DR   HOGENOM; CLU_000604_92_3_4; -.
DR   Proteomes; UP000001930; Chromosome I.
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; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..506
FT                   /note="Ribose import ATP-binding protein RbsA 1"
FT                   /id="PRO_0000261052"
FT   DOMAIN          5..241
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          254..498
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   506 AA;  55306 MW;  09E7701AE0EDE306 CRC64;
     MDTILALTGI TKRFPGVVAL RGIDLRVARG EIHALLGENG AGKSTLMKIL CGIYPPDEGT
     IAIDGEPRRF ANHHDAIAAG VGIVFQEFSL IPDLNAVDNL FLGREWRGRL GLRDRARMRR
     AAADIFARLG MAVDLSAPVR ELSVAQQQFV EIGKALSLDA RVLILDEPTA TLTPAEAARL
     FGVMRELKRQ GVAMIFISHH LDEIFEVCDR ITVLRDGQYV GTTQRARTDV GALVEMMVGR
     RIEHSFPPKP PLARDAAAVL EVDALQVREN GPVNRFALRE GEILGFAGLV GSGRTSSALA
     LIGAKPARVR RMRLRGRAVR LSGPADALAA GIGLLPESRK TQGLITEFSI RHNVAINNLG
     KHRRLRWFVD AAAEARATRE LMKRLGVKAP TPDTRVDTLS GGNQQKVVIA RWLNHHTRIL
     IFDEPTRGID IGAKAEIYQL MRELTARGYS IVLISSELPE IVGMCDRVAV FRQGRIEAVL
     DGDAIDANTV MTYATSDARG ANHEHA
 
 
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