ID   RIBU_LACLM              Reviewed;         206 AA.
AC   P0CI36; A2RKH8; Q1RN04;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Riboflavin transporter RibU;
DE   AltName: Full=Riboflavin ECF transporter S component RibU;
GN   Name=ribU; OrderedLocusNames=llmg_1195;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [2]
RP   SUBUNIT, SUBCELLULAR LOCATION, EXPRESSION IN E.COLI, AND FUNCTION.
RC   STRAIN=MG1363;
RX   PubMed=21135102; DOI=10.1074/jbc.m110.199224;
RA   ter Beek J., Duurkens R.H., Erkens G.B., Slotboom D.J.;
RT   "Quaternary structure and functional unit of energy coupling factor (ECF)-
RT   type transporters.";
RL   J. Biol. Chem. 286:5471-5475(2011).
CC   -!- FUNCTION: Mediates riboflavin uptake, may also transport FMN and
CC       roseoflavin (By similarity). Probably a riboflavin-binding protein that
CC       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. Uptake of riboflavin into proteosomes containing
CC       EcfA1A2T and RibU has been demonstrated. Uptake requires hydrolyzable
CC       Mg-ATP. {ECO:0000250, ECO:0000269|PubMed:21135102}.
CC   -!- SUBUNIT: In E.coli forms a stable energy-coupling factor (ECF)
CC       transporter complex composed of 2 membrane-embedded substrate-binding
CC       protein (S component), 2 ATP-binding proteins (A and A' components) and
CC       2 transmembrane proteins (T component), probably with a stoichiometry
CC       of 2:1:1:2. May be able to interact with more than 1 S component at a
CC       time. {ECO:0000269|PubMed:21135102}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21135102};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
CC   -!- DOMAIN: Riboflavin is stacked with one or more Trp residues in the
CC       binding pocket of RibU. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic riboflavin transporter (P-RFT)
CC       (TC 2.A.87) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM406671; CAL97788.1; -; Genomic_DNA.
DR   RefSeq; WP_011835093.1; NZ_WJVF01000010.1.
DR   AlphaFoldDB; P0CI36; -.
DR   SMR; P0CI36; -.
DR   STRING; 416870.llmg_1195; -.
DR   EnsemblBacteria; CAL97788; CAL97788; llmg_1195.
DR   GeneID; 61109529; -.
DR   KEGG; llm:llmg_1195; -.
DR   eggNOG; COG3601; Bacteria.
DR   HOGENOM; CLU_086673_2_1_9; -.
DR   OMA; MFLEFPI; -.
DR   PhylomeDB; P0CI36; -.
DR   BioCyc; LLAC416870:LLMG_RS06050-MON; -.
DR   Proteomes; UP000000364; 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:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:GO_Central.
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   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..206
FT                   /note="Riboflavin transporter RibU"
FT                   /id="PRO_0000397873"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   206 AA;  22972 MW;  FB21E947396E2FB3 CRC64;
     MSKTRRMVLI AMLAALSTIL LLPILQFPLL PGIDFMKVEL SIIPVLIGVF TLGLGDGFII
     LFIRSVLWYL LFNQGPSTWI GVPMNFVALG IFMAIVWFFT KKKFSIKNYT VGIVLATIAS
     VLVMMVLNVF YALPLYRLAA GFDVDKIFAG ATHLFNMGSL SVTLNPTYLL TVVLPFNALQ
     YIIFALVFGL IVTVFKKNKV VKFYNA