ID   RIBZ_CLOD6              Reviewed;         456 AA.
AC   Q180E3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Riboflavin transporter RibZ {ECO:0000305};
GN   Name=ribZ {ECO:0000303|PubMed:25938806};
GN   OrderedLocusNames=CD630_32990 {ECO:0000312|EMBL:CAJ70196.1};
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
RN   [2]
RP   FUNCTION AS A TRANSPORTER, AND INDUCTION.
RC   STRAIN=630;
RX   PubMed=25938806; DOI=10.1371/journal.pone.0126124;
RA   Gutierrez-Preciado A., Torres A.G., Merino E., Bonomi H.R., Goldbaum F.A.,
RA   Garcia-Angulo V.A.;
RT   "Extensive identification of bacterial riboflavin transporters and their
RT   distribution across bacterial species.";
RL   PLoS ONE 10:E0126124-E0126124(2015).
CC   -!- FUNCTION: Transports riboflavin into the cell.
CC       {ECO:0000269|PubMed:25938806}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is probably regulated by riboflavin, via an FMN
CC       riboswitch. {ECO:0000269|PubMed:25938806}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM180355; CAJ70196.1; -; Genomic_DNA.
DR   RefSeq; WP_003435615.1; NZ_CP010905.2.
DR   RefSeq; YP_001089815.1; NC_009089.1.
DR   AlphaFoldDB; Q180E3; -.
DR   SMR; Q180E3; -.
DR   STRING; 272563.CD630_32990; -.
DR   TCDB; 2.A.1.3.72; the major facilitator superfamily (mfs).
DR   EnsemblBacteria; CAJ70196; CAJ70196; CD630_32990.
DR   GeneID; 66355793; -.
DR   KEGG; cdf:CD630_32990; -.
DR   KEGG; pdc:CDIF630_03600; -.
DR   PATRIC; fig|272563.120.peg.3484; -.
DR   eggNOG; COG2814; Bacteria.
DR   OMA; TMRNVDP; -.
DR   PhylomeDB; Q180E3; -.
DR   BioCyc; PDIF272563:G12WB-3466-MON; -.
DR   Proteomes; UP000001978; Chromosome.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR004638; EmrB-like.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00711; efflux_EmrB; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..456
FT                   /note="Riboflavin transporter RibZ"
FT                   /id="PRO_0000438275"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   456 AA;  49388 MW;  6DADDCA9CF70A0FC CRC64;
     MKQKWIVLII ICIGVFMSTL DGSILNIANP TIAADFKINM SQIQWVVTAY MLVVTATMLF
     FGKLGDKVGS NRLYTLGFFI FTIGSFLCSM SNNLSTLISS RIFQAVGASI LMATGLGIVS
     NAFPANEKGK AIGITGAVVG IGNMSGPVIG GIILEHFGWP SIFIINIPIG IIAVFLGIKF
     LPKPVLDEQN KSFDIPGLLL FASCTTLILL AMNEKGNTRL YLGITALIIF LLLALREVKF
     EQSFIDLPLF KNRNFTVGNI IGVACYFPQM AVSFLLPFYL EQLKNLSPMM AGYVMTVHPL
     IMVLIAPIAG SLSDKHGAKN ILTASFSFMT ISLVGMALLK ADSPLYLLIV CLVIFGLGLG
     AFSSPNNSSI LADVPPQKQG YGGSFLATIR NLSFALGTAF FSSFFAQSLT YNQKFKSHTS
     AYVIASNQSY WIAASVCFIG LILTVFFMRK TDKSIS