ID   RIBU_STRT2              Reviewed;         211 AA.
AC   Q5M614;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Riboflavin transporter RibU;
DE   AltName: Full=Riboflavin ECF transporter S component RibU;
GN   Name=ribU; OrderedLocusNames=stu0268;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
RN   [2]
RP   FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   EXPRESSION IN E.COLI.
RC   STRAIN=ATCC BAA-250 / LMG 18311;
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. {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), 2 ATP-binding proteins (A component) and 2 transmembrane
CC       proteins (T component) upon coexpression of the 4 components in E.coli.
CC       {ECO:0000269|PubMed:23359690}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23359690};
CC       Multi-pass membrane protein {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; CP000023; AAV59992.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5M614; -.
DR   SMR; Q5M614; -.
DR   STRING; 264199.stu0268; -.
DR   TCDB; 3.A.1.25.6; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAV59992; AAV59992; stu0268.
DR   KEGG; stl:stu0268; -.
DR   eggNOG; COG3601; Bacteria.
DR   HOGENOM; CLU_086673_2_1_9; -.
DR   OMA; MFLEFPI; -.
DR   Proteomes; UP000001170; 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   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..211
FT                   /note="Riboflavin transporter RibU"
FT                   /id="PRO_0000422261"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   211 AA;  23644 MW;  944B2B32A43E6E03 CRC64;
     MRSLFFGIGK SIGNFFQIVK IWRNFFMTNT RKLAYIAILS AVSFLLLYFS FPLIPAADFL
     KVDFSILPVL IALVIFDFKS AIGVLLLRSL LKLLLNNGGP GSMIGLPMNF VALGVFVWGL
     SYFWKKNQTS KNYILGSVLG TILLTVAMVV LNYIYAVPLY AKFANFDIAQ FIGLYKYLFA
     MVVPFNLLEG LIFSVAFALI YAPLKSILVK L