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RFUB_TREPA
ID   RFUB_TREPA              Reviewed;         586 AA.
AC   O83321; O83322;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Probable riboflavin import ATP-binding protein RfuB {ECO:0000305};
DE            EC=7.6.2.- {ECO:0000305};
GN   Name=rfuB {ECO:0000303|PubMed:23404400}; OrderedLocusNames=TP_0299/TP_0300;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
RN   [2]
RP   IDENTIFICATION OF FRAMESHIFT, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=23404400; DOI=10.1128/mbio.00615-12;
RA   Deka R.K., Brautigam C.A., Biddy B.A., Liu W.Z., Norgard M.V.;
RT   "Evidence for an ABC-type riboflavin transporter system in pathogenic
RT   spirochetes.";
RL   MBio 4:E00615-E00615(2013).
CC   -!- FUNCTION: Probably part of the ABC transporter complex RfuABCD involved
CC       in riboflavin import. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000305|PubMed:23404400}.
CC   -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC       (RfuB), two transmembrane proteins (RfuC and RfuD) and a solute-binding
CC       protein (RfuA). {ECO:0000305|PubMed:23404400}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:23404400}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:23404400}; Cytoplasmic side
CC       {ECO:0000305|PubMed:23404400}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC65288.1; Type=Frameshift; Evidence={ECO:0000305|PubMed:23404400};
CC       Sequence=AAC65293.1; Type=Frameshift; Evidence={ECO:0000305|PubMed:23404400};
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DR   EMBL; AE000520; AAC65293.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE000520; AAC65288.1; ALT_FRAME; Genomic_DNA.
DR   PIR; E71341; E71341.
DR   RefSeq; WP_014342787.1; NC_021490.2.
DR   AlphaFoldDB; O83321; -.
DR   STRING; 243276.TPANIC_0300; -.
DR   EnsemblBacteria; AAC65288; AAC65288; TP_0300.
DR   EnsemblBacteria; AAC65293; AAC65293; TP_0299.
DR   KEGG; tpa:TP_0299; -.
DR   KEGG; tpa:TP_0300; -.
DR   PATRIC; fig|243276.5.peg.318; -.
DR   eggNOG; COG3845; Bacteria.
DR   HOGENOM; CLU_2686724_0_0_12; -.
DR   Proteomes; UP000000811; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..586
FT                   /note="Probable riboflavin import ATP-binding protein RfuB"
FT                   /id="PRO_0000202229"
FT   DOMAIN          46..299
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          343..586
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   586 AA;  64410 MW;  86C8FFE4D416A329 CRC64;
     MMIAERGVRA SARGVLSLHH IGKTYPRVMP RSKRGVWGMF GHPGRRAVDD AHTAHGPCSG
     ARETDAAEHS VLSDVNLSFF TGEIHALLGK NGAGKSTLAH ILSGFCVPTH GQLRLDGKEQ
     RFSVPFDALR AGIGIVHQQP VFAERATVFE NVVMGSAALT GVRWVRRAQV RERIDRIIAQ
     WRMPLKKEEY VACLSADKRF FVSLLCVLFR NPRFIILDEP RCAPAQSRAV FFSHLEEFFV
     RSSHAPRCGG GVIVVTHRFA DALRWAQRIS LIEGGKACSF LRTDLLDEYC SAHQVNECIQ
     KVSCALMSAS TVTSSAVSSF SSLSDTQSCA TVPRTSSARP WVLRVESLQV SKHADVPLTD
     ISFSVAASAI IGIVGTPEDG VHVLEDILCD MHAGASRTHC TGNILLQEHD QVWCLPLQRN
     TPSLLRAHGV ACVPSNCIQR GASMQLTLFD LLVPYTLRTW RTRVRAQMRF VARLLAEEEI
     YCDPLQPACT LSGGQLQRVI LARELATRPR LLILAEPAEG LDSASEQRLL ARLRQVAQAG
     TALVLLAREQ HQAQWRALCT ERFLLRAGTL CAEVSGTPSP SQDSHT
 
 
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