RIBU_LACLN
ID RIBU_LACLN Reviewed; 206 AA.
AC D8KIE9; A2RKH8; Q1RN04;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Riboflavin transporter RibU;
DE AltName: Full=Riboflavin ECF transporter S component RibU;
GN Name=ribU; OrderedLocusNames=LLNZ_06150;
OS Lactococcus lactis subsp. cremoris (strain NZ9000).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=746361;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A TRANSPORTER, ACTIVITY
RP REGULATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NZ9000;
RX PubMed=16585736; DOI=10.1128/jb.188.8.2752-2760.2006;
RA Burgess C.M., Slotboom D.J., Geertsma E.R., Duurkens R.H., Poolman B.,
RA van Sinderen D.;
RT "The riboflavin transporter RibU in Lactococcus lactis: molecular
RT characterization of gene expression and the transport mechanism.";
RL J. Bacteriol. 188:2752-2760(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ9000;
RX PubMed=20639323; DOI=10.1128/jb.00533-10;
RA Linares D.M., Kok J., Poolman B.;
RT "Genome sequences of Lactococcus lactis MG1363 (revised) and NZ9000 and
RT comparative physiological studies.";
RL J. Bacteriol. 192:5806-5812(2010).
RN [3]
RP SUBCELLULAR LOCATION, DOMAIN, RIBOFLAVIN-BINDING, AND MUTAGENESIS OF
RP TRP-68; TRP-79 AND TRP-97.
RC STRAIN=NZ9000;
RX PubMed=17289680; DOI=10.1074/jbc.m608583200;
RA Duurkens R.H., Tol M.B., Geertsma E.R., Permentier H.P., Slotboom D.J.;
RT "Flavin binding to the high affinity riboflavin transporter RibU.";
RL J. Biol. Chem. 282:10380-10386(2007).
CC -!- FUNCTION: Probably a riboflavin-binding protein that interacts with the
CC energy-coupling factor (ECF) ABC-transporter complex. Unlike classic
CC ABC transporters this ECF transporter provides the energy necessary to
CC transport a number of different substrates. The substrates themselves
CC are bound by transmembrane, not extracytoplasmic soluble proteins (By
CC similarity). Mediates riboflavin uptake, probably also transports FMN
CC and roseoflavin. {ECO:0000250, ECO:0000269|PubMed:16585736}.
CC -!- ACTIVITY REGULATION: Inhibited by FMN and roseoflavin.
CC {ECO:0000269|PubMed:16585736}.
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:17289680};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17289680}.
CC -!- INDUCTION: Induced by riboflavin deficiency.
CC {ECO:0000269|PubMed:16585736}.
CC -!- DOMAIN: Riboflavin is stacked with one or more Trp residues in the
CC binding pocket of RibU. {ECO:0000269|PubMed:17289680}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits altered transcriptional control
CC of the riboflavin biosynthesis operon in response to riboflavin and
CC FMN, and does not consume riboflavin from the growth medium.
CC {ECO:0000269|PubMed:16585736}.
CC -!- MISCELLANEOUS: Riboflavin, FMN and roseoflavin, but not FAD, bind to
CC RibU with high affinity and 1:1 stoichiometry.
CC -!- SIMILARITY: Belongs to the prokaryotic riboflavin transporter (P-RFT)
CC (TC 2.A.87) family. {ECO:0000305}.
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DR EMBL; AY994156; AAY43361.1; -; Genomic_DNA.
DR EMBL; CP002094; ADJ60195.1; -; Genomic_DNA.
DR RefSeq; WP_011835093.1; NC_017949.1.
DR AlphaFoldDB; D8KIE9; -.
DR SMR; D8KIE9; -.
DR GeneID; 61109529; -.
DR KEGG; lln:LLNZ_06150; -.
DR PATRIC; fig|746361.3.peg.1235; -.
DR HOGENOM; CLU_086673_2_1_9; -.
DR OMA; MFLEFPI; -.
DR OrthoDB; 1497256at2; -.
DR BioCyc; LLAC746361:LLNZ_RS06055-MON; -.
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 Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..206
FT /note="Riboflavin transporter RibU"
FT /id="PRO_0000402187"
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"
FT MUTAGEN 68
FT /note="W->Y: Strong increase of the riboflavin dissociation
FT constant."
FT /evidence="ECO:0000269|PubMed:17289680"
FT MUTAGEN 79
FT /note="W->Y: No change in riboflavin binding."
FT /evidence="ECO:0000269|PubMed:17289680"
FT MUTAGEN 97
FT /note="W->Y: No change in riboflavin binding."
FT /evidence="ECO:0000269|PubMed:17289680"
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
