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RBSA_BACSU
ID   RBSA_BACSU              Reviewed;         493 AA.
AC   P36947; P96732;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 152.
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=BSU35940;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7921236; DOI=10.1099/13500872-140-8-1829;
RA   Woodson K., Devine K.M.;
RT   "Analysis of a ribose transport operon from Bacillus subtilis.";
RL   Microbiology 140:1829-1838(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA   Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA   Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA   Kunst F., Danchin A., Glaser P.;
RT   "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT   degrees).";
RL   Microbiology 143:3313-3328(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; Z25798; CAA81051.1; -; Genomic_DNA.
DR   EMBL; Z92953; CAB07463.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15611.1; -; Genomic_DNA.
DR   PIR; H69689; H69689.
DR   RefSeq; NP_391475.1; NC_000964.3.
DR   RefSeq; WP_003244379.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P36947; -.
DR   SMR; P36947; -.
DR   STRING; 224308.BSU35940; -.
DR   jPOST; P36947; -.
DR   PaxDb; P36947; -.
DR   PRIDE; P36947; -.
DR   DNASU; 936839; -.
DR   EnsemblBacteria; CAB15611; CAB15611; BSU_35940.
DR   GeneID; 936839; -.
DR   KEGG; bsu:BSU35940; -.
DR   PATRIC; fig|224308.179.peg.3891; -.
DR   eggNOG; COG1129; Bacteria.
DR   InParanoid; P36947; -.
DR   OMA; AKREIYQ; -.
DR   PhylomeDB; P36947; -.
DR   BioCyc; BSUB:BSU35940-MON; -.
DR   Proteomes; UP000001570; 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; 2.
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..493
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000092955"
FT   DOMAIN          3..239
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          246..493
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"
FT   CONFLICT        43
FT                   /note="T -> R (in Ref. 1; CAA81051)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327..383
FT                   /note="GLGFITENRKDEGLLLDTSIRENIALPNLSSFSPKGLIDHKREAEFVDLLIK
FT                   RLTIK -> VSALLQRIARMKGSCS (in Ref. 1; CAA81051)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398..400
FT                   /note="NQQ -> KPGK (in Ref. 1; CAA81051)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  54532 MW;  48AACF3315FC69D6 CRC64;
     MQIEMKDIHK TFGKNQVLSG VSFQLMPGEV HALMGENGAG KSTLMNILTG LHKADKGQIS
     INGNETYFSN PKEAEQHGIA FIHQELNIWP EMTVLENLFI GKEISSKLGV LQTRKMKALA
     KEQFDKLSVS LSLDQEAGEC SVGQQQMIEI AKALMTNAEV IIMDEPTAAL TEREISKLFE
     VITALKKNGV SIVYISHRME EIFAICDRIT IMRDGKTVDT TNISETDFDE VVKKMVGREL
     TERYPKRTPS LGDKVFEVKN ASVKGSFEDV SFYVRSGEIV GVSGLMGAGR TEMMRALFGV
     DRLDTGEIWI AGKKTAIKNP QEAVKKGLGF ITENRKDEGL LLDTSIRENI ALPNLSSFSP
     KGLIDHKREA EFVDLLIKRL TIKTASPETH ARHLSGGNQQ KVVIAKWIGI GPKVLILDEP
     TRGVDVGAKR EIYTLMNELT ERGVAIIMVS SELPEILGMS DRIIVVHEGR ISGEIHAREA
     TQERIMTLAT GGR
 
 
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