ID   RIBU_STAAH              Reviewed;         189 AA.
AC   E5QVT2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Riboflavin transporter RibU;
DE   AltName: Full=Riboflavin ECF transporter S component RibU;
GN   Name=ribU; OrderedLocusNames=HMPREF0772_11721;
OS   Staphylococcus aureus (strain TCH60).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=548473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCH60;
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RT   "Complete genome sequence of Staphylococcus aureus strain TCH60.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   STRAIN=TCH60;
RX   PubMed=20972419; DOI=10.1038/nature09488;
RA   Zhang P., Wang J., Shi Y.;
RT   "Structure and mechanism of the S component of a bacterial ECF
RT   transporter.";
RL   Nature 468:717-720(2010).
CC   -!- FUNCTION: Mediates riboflavin uptake, may also transport FMN and
CC       roseoflavin. Probably a riboflavin-binding protein that interacts with
CC       the energy-coupling factor (ECF) ABC-transporter complex. Unlike
CC       classic ABC transporters this ECF transporter provides the energy
CC       necessary to transport a number of different substrates. The substrates
CC       themselves are bound by transmembrane, not extracytoplasmic soluble
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC       complex composed of a membrane-embedded substrate-binding protein (S
CC       component), 2 ATP-binding proteins (A component) and 2 transmembrane
CC       proteins (T component). May be able to interact with more than 1 S
CC       component at a time (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20972419};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:20972419}.
CC   -!- SIMILARITY: Belongs to the prokaryotic riboflavin transporter (P-RFT)
CC       (TC 2.A.87) family. {ECO:0000305}.
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DR   EMBL; CP002110; ADQ77183.1; -; Genomic_DNA.
DR   PDB; 3P5N; X-ray; 3.60 A; A/B=1-189.
DR   PDBsum; 3P5N; -.
DR   AlphaFoldDB; E5QVT2; -.
DR   SMR; E5QVT2; -.
DR   KEGG; suq:HMPREF0772_11721; -.
DR   PATRIC; fig|548473.6.peg.1680; -.
DR   HOGENOM; CLU_086673_2_2_9; -.
DR   OMA; MFLEFPI; -.
DR   EvolutionaryTrace; E5QVT2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; IEA:InterPro.
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 membrane; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..189
FT                   /note="Riboflavin transporter RibU"
FT                   /id="PRO_0000407286"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..44
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        45..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..82
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..159
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..189
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   189 AA;  21009 MW;  40B3933B67895D2E CRC64;
     MNGRRKLNMQ QNKRLITISM LSAIAFVLTF IKFPIPFLPP YLTLDFSDVP SLLATFTFGP
     VAGIIVALVK NLLNYLFSMG DPVGPFANFL AGASFLLTAY AIYKNKRSTK SLITGLIIAT
     IVMTIVLSIL NYFVLLPLYG MIFNLADIAN NLKVIIVSGI IPFNIIKGIV ISIVFILLYR
     RLANFLKRI