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RBSA_ALKHC
ID   RBSA_ALKHC              Reviewed;         499 AA.
AC   Q9K6J9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=BH3730;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01716};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; BA000004; BAB07449.1; -; Genomic_DNA.
DR   PIR; B84116; B84116.
DR   AlphaFoldDB; Q9K6J9; -.
DR   SMR; Q9K6J9; -.
DR   STRING; 272558.10176354; -.
DR   PRIDE; Q9K6J9; -.
DR   EnsemblBacteria; BAB07449; BAB07449; BAB07449.
DR   KEGG; bha:BH3730; -.
DR   eggNOG; COG1129; Bacteria.
DR   HOGENOM; CLU_000604_92_3_9; -.
DR   OMA; AKREIYQ; -.
DR   Proteomes; UP000001258; Chromosome.
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 membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..499
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000261041"
FT   DOMAIN          3..240
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          250..494
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   499 AA;  54985 MW;  57CFB940C4C79E11 CRC64;
     MIVEMTGIHK SFSGNPVLKD VSFTLEKGEI HALMGENGAG KSTLMKILTG IYERDSGTVK
     IKGREVHYKH PKEAEADGLA VIHQELNILP ELTVAENLFV GKERTYGKTG WIKSKEMNRL
     AEEKLAELGL KVKGTERAGN LSVGKQQLIE IAKALMTNAD IIIMDEPTAA LTDREIDTLF
     ATVRELQKKG VTFVYISHRM EEIFSLCQRI TVLRDGEYVG TKVIAETSFD EIVKMMVGRA
     LGNRFPEHTL TPGDVKLEIK HLTRAGEFEN VSLSVRAGEI LGISGLMGAG RSELVETIFG
     YRKADSGEVW IDGKQAAIKG PDQAIAQGIG FVSEDRKSKG LIVDFSIRDN ISLTNLSRIS
     TSSWISSEKE RSLYEELAKK LHVKASGPSQ QAKSLSGGNQ QKIVIAKWLG IEPKILILDE
     PTRGVDVGAK KEIYTIMNEL AKQGVAIIMV SSELPEVIGL STRVAVMFEG KLMHILERDE
     LSEETIMHYA TGGDKHVRQ
 
 
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