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RBSA1_STRAW
ID   RBSA1_STRAW             Reviewed;         522 AA.
AC   Q82CM5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=SAV_5319;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC73031.1; -; Genomic_DNA.
DR   RefSeq; WP_010986723.1; NZ_JZJK01000072.1.
DR   AlphaFoldDB; Q82CM5; -.
DR   SMR; Q82CM5; -.
DR   STRING; 227882.SAV_5319; -.
DR   EnsemblBacteria; BAC73031; BAC73031; SAVERM_5319.
DR   KEGG; sma:SAVERM_5319; -.
DR   eggNOG; COG1129; Bacteria.
DR   HOGENOM; CLU_000604_92_0_11; -.
DR   OMA; IKMLSGA; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000000428; 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..522
FT                   /note="Ribose import ATP-binding protein RbsA 1"
FT                   /id="PRO_0000261108"
FT   DOMAIN          8..243
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          249..496
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   REGION          492..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   522 AA;  55641 MW;  B69A182E5EB9689A CRC64;
     MSNADELLRI EGIRKTFPGV VALDGVDFDL RRGEVHVLLG ENGAGKSTLI KMLSGAYRPD
     GGRVLVEGEE VRIHGAQDSE ALGIATIYQE FNLVPDLTVA ENIFLGRQPR RLGLIDRKKM
     EADAAELLAR VGVQVSPRAR VRELGIARLQ MVEIAKALSL NARVLIMDEP TAVLTSEEVE
     KLFAIVRQLR EDGVGIVFIT HHLEEIAALG DRVTVIRDGK SVGQVPASTS EDELVRLMVG
     RSIEQQYPRE RPDSGAALLS VEGLTRDGVF HDVSFEVRAG EVVGVAGLVG AGRTEVVRAV
     FGADPYDRGS VQVAGARVPR HDVSAAMSAG IGLVPEDRKG QGLVLDASVE ENLGLVTMRA
     ATRGGLVDLK GQRDAAARVA GQLGVRMAGL GQHVRTLSGG NQQKVVIGKW LLADTKVLIL
     DEPTRGIDVG AKVEIYQLIN ELTAAGAAVL MISSDLPEVL GMSDRVLVMA QGRIAGELGA
     DEATQDSVMA LAVSTNQYKP DKSDKPDASA GKTDQKEAPR GH
 
 
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