RIBU_THEMA
ID RIBU_THEMA Reviewed; 183 AA.
AC Q9X1G6; G4FFJ0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Riboflavin transporter RibU;
DE AltName: Full=Riboflavin ECF transporter S component RibU;
GN Name=ribU; OrderedLocusNames=TM_1455;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, AND
RP EXPRESSION IN E.COLI.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23359690; DOI=10.1073/pnas.1217361110;
RA Karpowich N.K., Wang D.N.;
RT "Assembly and mechanism of a group II ECF transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013).
CC -!- FUNCTION: Substrate-binding (S) component of an energy-coupling factor
CC (ECF) ABC-transporter complex. Mediates riboflavin uptake, may also
CC transport FMN and roseoflavin. Probably a riboflavin-binding protein
CC that interacts with the energy-coupling factor (ECF) ABC-transporter
CC complex. Unlike classic ABC transporters this ECF transporter provides
CC the energy necessary to transport a number of different substrates. The
CC substrates themselves are bound by transmembrane, not extracytoplasmic
CC soluble proteins (Probable). Expression of the complex plus RibU in
CC E.coli allows riboflavin uptake; uptake does not occur in the absence
CC of RibU or the EcfA1A2T complex. {ECO:0000269|PubMed:23359690,
CC ECO:0000305}.
CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC complex composed of 2 membrane-embedded substrate-binding proteins (S
CC component, RibU, BioY), 2 ATP-binding proteins (A component) and 2
CC transmembrane proteins (T component) upon coexpression in E.coli. A
CC stable subcomplex with both A and T components are also isolated. This
CC complex interacts with at least 2 substrate-specific components, BioY
CC and RibU. {ECO:0000269|PubMed:23359690}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:23359690}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:23359690}.
CC -!- SIMILARITY: Belongs to the prokaryotic riboflavin transporter (P-RFT)
CC (TC 2.A.87) family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36523.1; -; Genomic_DNA.
DR PIR; H72250; H72250.
DR RefSeq; NP_229254.1; NC_000853.1.
DR RefSeq; WP_004081740.1; NZ_CP011107.1.
DR PDB; 5KBW; X-ray; 2.61 A; A/B=2-173.
DR PDB; 5KC0; X-ray; 3.20 A; A=1-183.
DR PDB; 5KC4; X-ray; 3.40 A; A/E=2-173.
DR PDBsum; 5KBW; -.
DR PDBsum; 5KC0; -.
DR PDBsum; 5KC4; -.
DR AlphaFoldDB; Q9X1G6; -.
DR SMR; Q9X1G6; -.
DR STRING; 243274.THEMA_07040; -.
DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAD36523; AAD36523; TM_1455.
DR KEGG; tma:TM1455; -.
DR eggNOG; COG3601; Bacteria.
DR InParanoid; Q9X1G6; -.
DR OMA; MFLEFPI; -.
DR OrthoDB; 1497256at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IGI:UniProtKB.
DR GO; GO:0032218; P:riboflavin transport; IGI:UniProtKB.
DR InterPro; IPR024529; ECF_trnsprt_substrate-spec.
DR InterPro; IPR025720; RibU.
DR PANTHER; PTHR38438; PTHR38438; 1.
DR Pfam; PF12822; ECF_trnsprt; 1.
DR PIRSF; PIRSF037778; UCP037778_transp_RibU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..183
FT /note="Riboflavin transporter RibU"
FT /id="PRO_0000422262"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:5KBW"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:5KBW"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5KBW"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:5KBW"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:5KBW"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:5KBW"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:5KBW"
FT HELIX 101..131
FT /evidence="ECO:0007829|PDB:5KBW"
FT HELIX 135..170
FT /evidence="ECO:0007829|PDB:5KBW"
SQ SEQUENCE 183 AA; 20015 MW; BFCB532C18F64DB6 CRC64;
MSSIKKISFV GIFSALATLV MFLEFPIFPQ ASFLKYDPSE IPALIVSFLL GPGVGMFVVL
VKDILFFLMK SGDPVGIAMN AVLGMSFVGI AGLIYHRNKS RATAIKGMIV ATLFATAFAL
GLNALIVPLY FEAPFELYLK FFPFILAFNL VKFGIDSVVT FFVYKKVSSI LKLETVEGRS
NNG
