RIBY_CHLAA
ID RIBY_CHLAA Reviewed; 351 AA.
AC A9WGD2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Riboflavin-binding protein RibY {ECO:0000305};
DE Flags: Precursor;
GN Name=ribY {ECO:0000303|PubMed:25345570, ECO:0000303|PubMed:25938806};
GN OrderedLocusNames=Caur_0817 {ECO:0000312|EMBL:ABY34053.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
RN [2]
RP SUBUNIT, AND RIBOFLAVIN BINDING.
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=25345570; DOI=10.1111/1758-2229.12227;
RA Rodionova I.A., Li X., Plymale A.E., Motamedchaboki K., Konopka A.E.,
RA Romine M.F., Fredrickson J.K., Osterman A.L., Rodionov D.A.;
RT "Genomic distribution of B-vitamin auxotrophy and uptake transporters in
RT environmental bacteria from the Chloroflexi phylum.";
RL Environ. Microbiol. Rep. 7:204-210(2015).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
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: Part of an ABC transporter complex that transports riboflavin
CC into the cell (PubMed:25938806). Binds riboflavin (PubMed:25345570).
CC {ECO:0000269|PubMed:25345570, ECO:0000269|PubMed:25938806}.
CC -!- SUBUNIT: The complex is likely composed of an ATP-binding protein, a
CC transmembrane protein (RibX) and a solute-binding protein (RibY).
CC {ECO:0000305|PubMed:25345570}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Expression is probably regulated by riboflavin, via an FMN
CC riboswitch. {ECO:0000269|PubMed:25938806}.
CC -!- SIMILARITY: Belongs to the NMT1 family. {ECO:0000305}.
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DR EMBL; CP000909; ABY34053.1; -; Genomic_DNA.
DR RefSeq; WP_012256709.1; NC_010175.1.
DR RefSeq; YP_001634442.1; NC_010175.1.
DR AlphaFoldDB; A9WGD2; -.
DR SMR; A9WGD2; -.
DR STRING; 324602.Caur_0817; -.
DR TCDB; 3.A.1.17.14; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABY34053; ABY34053; Caur_0817.
DR KEGG; cau:Caur_0817; -.
DR PATRIC; fig|324602.8.peg.931; -.
DR eggNOG; COG0715; Bacteria.
DR HOGENOM; CLU_028871_1_0_0; -.
DR InParanoid; A9WGD2; -.
DR OMA; YVMAMYQ; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR027939; NMT1/THI5.
DR InterPro; IPR015168; SsuA/THI5.
DR PANTHER; PTHR31528; PTHR31528; 1.
DR Pfam; PF09084; NMT1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..351
FT /note="Riboflavin-binding protein RibY"
FT /id="PRO_5002745825"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 351 AA; 37700 MW; 21441938532CE4A2 CRC64;
MMKLRVLTLG ILIILLITAC SAPTPTTPAA APTAAPAPNA QPTLQQVTLA MSYIPNIQFA
PYYVAAAKGY YAAEGIEVVF DYNFENDVLQ RAATWPTSGV AFATTSGTSV LLARQQGLPV
KTVMTLYQRF PIAFFAKSNV PLASVNDLRG QTIGIPGRFG ESFYALLAAL YAGGMSEADV
TVQEIGFTQT AAVMEDKVPV AIGYAMNEPV QLRGQGVEVN VLLAADVFNL AANGIAVSEA
LIAQNPELVR KFVRASLRGL ADTLANPDEA FDLSLQFIPE AQLGDLSLQR QVLQESLPFW
QNELTAQYGL GYTDGQLWTR TEEFMRAAGL LSAPVDVQQA FTNEFVPGGS Y