(data stored in SCRATCH zone)

SWISSPROT: E6V2E8_VARPE

ID   E6V2E8_VARPE            Unreviewed;       505 AA.
AC   E6V2E8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000256|HAMAP-Rule:MF_01716};
DE            EC=3.6.3.17 {ECO:0000256|HAMAP-Rule:MF_01716};
GN   Name=rbsA {ECO:0000256|HAMAP-Rule:MF_01716};
GN   OrderedLocusNames=Varpa_0357 {ECO:0000313|EMBL:ADU34579.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34579.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34579.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34579.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in
CC       ribose import. Responsible for energy coupling to the transport
CC       system. {ECO:0000256|HAMAP-Rule:MF_01716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(2)O + monosaccharide(Out) = ADP + phosphate +
CC         monosaccharide(In).; EC=3.6.3.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01716, ECO:0000256|SAAS:SAAS01120535};
CC   -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA),
CC       two transmembrane proteins (RbsC) and a solute-binding protein
CC       (RbsB). {ECO:0000256|HAMAP-Rule:MF_01716}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01716}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01716}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose
CC       importer (TC 3.A.1.2.1) family. {ECO:0000256|HAMAP-Rule:MF_01716}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00434}.
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DR   EMBL; CP002417; ADU34579.1; -; Genomic_DNA.
DR   RefSeq; WP_013538825.1; NC_014931.1.
DR   STRING; 595537.Varpa_0357; -.
DR   EnsemblBacteria; ADU34579; ADU34579; Varpa_0357.
DR   GeneID; 29719276; -.
DR   KEGG; vpe:Varpa_0357; -.
DR   eggNOG; ENOG4105C2J; Bacteria.
DR   eggNOG; COG1129; LUCA.
DR   KO; K10441; -.
DR   OMA; AVENMFL; -.
DR   OrthoDB; 551294at2; -.
DR   BioCyc; VPAR595537:G1GQO-359-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015591; F:D-ribose transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR015861; ABC_transpr_RbsA.
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;
DR   PRODOM; E6V2E8.
DR   SWISS-2DPAGE; E6V2E8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01716, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00041633};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01716};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01716,
KW   ECO:0000256|SAAS:SAAS00436433};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01716,
KW   ECO:0000256|SAAS:SAAS00041638};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01716,
KW   ECO:0000256|SAAS:SAAS00436442};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01716,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00041632};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Repeat {ECO:0000256|SAAS:SAAS00041639};
KW   Sugar transport {ECO:0000256|HAMAP-Rule:MF_01716,
KW   ECO:0000256|SAAS:SAAS00041640};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01716,
KW   ECO:0000256|SAAS:SAAS00041634}.
FT   DOMAIN       11    247       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      260    503       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND      43     50       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   505 AA;  54654 MW;  C893F2F408B418B8 CRC64;
     MTSFAEGEEM LRLEGVSKRF PGVKALSGID LSIRKGEVHA LLGENGAGKS TLMKILGGIY
     QADEGRIFIE GSERRFAGYN DAIAAGIGII FQEFSLIPYL NAVENIFLGR YLKNRFGLMD
     KAGMKRSAER LFDELGVQID LDVPICRLSV AQQQFVEIGK ALSLKARLLV LDEPTATLTP
     NEAGHLFKIM RELRAKGVAM IFISHHLDEI FEVCDRISVL RDGANAGHAD VGATDVDALV
     EMMVGRRIEH NFPPKPQPAP RGRKVLEVPE IQLAKGGPVN SFTLHEGEIL GFAGLVGSGR
     TELALGMMGA DRVHRKTVLR NGKPVRLKDP TEALENGIGL LPESRKVEGL ITDFTVRFNI
     SMNNLGKHKS AGLVSQKSEK QSAGELAKRV GVKAPSIETR VATLSGGNQQ KVVIARWLGH
     ASEVLIFDEP TRGIDVGAKA EIYSLMRELT RQGKAIVMIS SELPEIVGMC DRVAVFSGGS
     IVATLEGDSI NSGDIMRHAT TGGSQ
//

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