FMNP_BACSU
ID FMNP_BACSU Reviewed; 190 AA.
AC P50726;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Riboflavin transporter FmnP;
DE AltName: Full=FMN permease;
DE AltName: Full=Riboflavin ECF transporter S component FmnP;
GN Name=fmnP; Synonyms=ribU, ypaA; OrderedLocusNames=BSU23050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION AS A TRANSPORTER, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17693491; DOI=10.1128/jb.00590-07;
RA Vogl C., Grill S., Schilling O., Stulke J., Mack M., Stolz J.;
RT "Characterization of riboflavin (vitamin B2) transport proteins from
RT Bacillus subtilis and Corynebacterium glutamicum.";
RL J. Bacteriol. 189:7367-7375(2007).
RN [4]
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=18931129; DOI=10.1128/jb.01208-08;
RA Rodionov D.A., Hebbeln P., Eudes A., ter Beek J., Rodionova I.A.,
RA Erkens G.B., Slotboom D.J., Gelfand M.S., Osterman A.L., Hanson A.D.,
RA Eitinger T.;
RT "A novel class of modular transporters for vitamins in prokaryotes.";
RL J. Bacteriol. 191:42-51(2009).
CC -!- FUNCTION: Mediates uptake of riboflavin and roseoflavin, a toxic
CC riboflavin analog; may also transport FMN. Probably a riboflavin-
CC binding protein that interacts with the energy-coupling factor (ECF)
CC ABC-transporter complex. Unlike classic ABC transporters this ECF
CC transporter provides the energy necessary to transport a number of
CC different substrates. The substrates themselves are bound by
CC transmembrane, not extracytoplasmic soluble proteins (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:17693491}.
CC -!- ACTIVITY REGULATION: Inhibited by excess of riboflavin or FMN. Also
CC inhibited by protonophores such as CCCP and FCCP or in the absence of
CC glucose. {ECO:0000269|PubMed:17693491}.
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:17693491};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17693491}.
CC -!- INDUCTION: Induced by riboflavin deficiency.
CC {ECO:0000269|PubMed:17693491}.
CC -!- DISRUPTION PHENOTYPE: Abolishes riboflavin uptake, cell growth less
CC inhibited by roseoflavin. {ECO:0000269|PubMed:18931129}.
CC -!- SIMILARITY: Belongs to the prokaryotic riboflavin transporter (P-RFT)
CC (TC 2.A.87) family. {ECO:0000305}.
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DR EMBL; L47648; AAC83944.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14237.1; -; Genomic_DNA.
DR PIR; E69932; E69932.
DR RefSeq; NP_390186.1; NC_000964.3.
DR RefSeq; WP_004399159.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P50726; -.
DR SMR; P50726; -.
DR STRING; 224308.BSU23050; -.
DR TCDB; 2.A.87.1.2; the prokaryotic riboflavin transporter (p-rft) family.
DR PaxDb; P50726; -.
DR EnsemblBacteria; CAB14237; CAB14237; BSU_23050.
DR GeneID; 938970; -.
DR KEGG; bsu:BSU23050; -.
DR PATRIC; fig|224308.179.peg.2512; -.
DR eggNOG; COG3601; Bacteria.
DR InParanoid; P50726; -.
DR OMA; MFLEFPI; -.
DR PhylomeDB; P50726; -.
DR BioCyc; BSUB:BSU23050-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0032218; P:riboflavin transport; IBA:GO_Central.
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..190
FT /note="Riboflavin transporter FmnP"
FT /id="PRO_0000049676"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 190 AA; 20553 MW; 35FF82AF1AFB2685 CRC64;
MKVKKLVVVS MLSSIAFVLM LLNFPFPGLP DYLKIDFSDV PAIIAILIYG PLAGIAVEAI
KNVLQYIIQG SMAGVPVGQV ANFIAGTLFI LPTAFLFKKL NSAKGLAVSL LLGTAAMTIL
MSILNYVLIL PAYTWFLHSP ALSDSALKTA VVAGILPFNM IKGIVITVVF SLIFIKLKPW
IEQQRSAHIH
