RFUA_TREPA
ID RFUA_TREPA Reviewed; 343 AA.
AC Q56328;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ABC transporter riboflavin-binding protein RfuA {ECO:0000305};
DE AltName: Full=Membrane lipoprotein TpN38(b) {ECO:0000305};
DE Flags: Precursor;
GN Name=rfuA {ECO:0000303|PubMed:23404400};
GN Synonyms=tpn38 {ECO:0000303|PubMed:8598278}; OrderedLocusNames=TP_0298;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=8598278; DOI=10.1111/j.1574-6968.1996.tb07966.x;
RA Stamm L.V., Hardham J.M., Frye J.G.;
RT "Expression and sequence analysis of a Treponema pallidum gene, Tpn38(b),
RT encoding an exported protein with homology to T. pallidum and Borrelia
RT burgdorferi proteins.";
RL FEMS Microbiol. Lett. 135:57-63(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [3] {ECO:0007744|PDB:4IIL}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-343 IN COMPLEX WITH
RP RIBOFLAVIN, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PALMITOYLATION AT
RP CYS-20, AND DIACYLGLYCEROL AT CYS-20.
RX PubMed=23404400; DOI=10.1128/mbio.00615-12;
RA Deka R.K., Brautigam C.A., Biddy B.A., Liu W.Z., Norgard M.V.;
RT "Evidence for an ABC-type riboflavin transporter system in pathogenic
RT spirochetes.";
RL MBio 4:E00615-E00615(2013).
CC -!- FUNCTION: Probably part of the ABC transporter complex RfuABCD involved
CC in riboflavin import. Binds riboflavin. {ECO:0000269|PubMed:23404400}.
CC -!- SUBUNIT: Monomer in solution (PubMed:23404400). The complex is probably
CC composed of two ATP-binding proteins (RfuB), two transmembrane proteins
CC (RfuC and RfuD) and a solute-binding protein (RfuA) (Probable).
CC {ECO:0000269|PubMed:23404400, ECO:0000305|PubMed:23404400}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:23404400}; Lipid-anchor
CC {ECO:0000305|PubMed:23404400}; Periplasmic side
CC {ECO:0000305|PubMed:23404400}.
CC -!- SIMILARITY: Belongs to the BMP lipoprotein 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; U12861; AAB02167.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65287.1; -; Genomic_DNA.
DR PIR; D71341; D71341.
DR RefSeq; WP_010881747.1; NC_021490.2.
DR PDB; 4IIL; X-ray; 1.30 A; A=21-343.
DR PDBsum; 4IIL; -.
DR AlphaFoldDB; Q56328; -.
DR SMR; Q56328; -.
DR IntAct; Q56328; 9.
DR STRING; 243276.TPANIC_0298; -.
DR EnsemblBacteria; AAC65287; AAC65287; TP_0298.
DR GeneID; 57878835; -.
DR KEGG; tpa:TP_0298; -.
DR eggNOG; COG1744; Bacteria.
DR HOGENOM; CLU_038813_0_1_12; -.
DR OMA; FRVVGNW; -.
DR OrthoDB; 603910at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR003760; PnrA-like.
DR Pfam; PF02608; Bmp; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..343
FT /note="ABC transporter riboflavin-binding protein RfuA"
FT /id="PRO_0000018008"
FT BINDING 43..46
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:23404400,
FT ECO:0007744|PDB:4IIL"
FT BINDING 124
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:23404400,
FT ECO:0007744|PDB:4IIL"
FT BINDING 140
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:23404400,
FT ECO:0007744|PDB:4IIL"
FT BINDING 176
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:23404400,
FT ECO:0007744|PDB:4IIL"
FT BINDING 208
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:23404400,
FT ECO:0007744|PDB:4IIL"
FT BINDING 255
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:23404400,
FT ECO:0007744|PDB:4IIL"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:23404400"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:23404400"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:4IIL"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4IIL"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:4IIL"
FT HELIX 320..335
FT /evidence="ECO:0007829|PDB:4IIL"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4IIL"
SQ SEQUENCE 343 AA; 37882 MW; 800687C5A1420C4D CRC64;
MNGAVCVLSA LIAVFTCFSC RPAVQDERAV RIAVFVPGFR HDSPVYAMLC DGVERAVTQE
RATGRSIGLD IIEAGPNQAL WREKLAHLAA EQRYRLIVSS NPALPHVLEP ILRQFPLQRF
LVLDAYAPQE HSLITFRYNQ WEQAYLAGHL SALVSASAMR FANADKKIGL IAGQSYPVMT
QTIIPAFLAG ARAVDPAFEV DVRVVGNWYD AAKSADLARI LFHEGVDVMM PICGGANQGV
LAAARELGFY VSWFDDNGYA RAPGYVVGSS VMEQERLAYE QTLRCIRGEL PSAGAWTLGV
KDGYVRFIEE DPLYLQTVPE PIRVRQSALL RRIQSGELTL PVR
