YKOF_BACSU
ID YKOF_BACSU Reviewed; 200 AA.
AC O34911; Q796L7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative HMP/thiamine-binding protein YkoF;
GN Name=ykoF; OrderedLocusNames=BSU13240;
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;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 IN HMP TRANSPORT.
RX PubMed=12376536; DOI=10.1074/jbc.m208965200;
RA Rodionov D.A., Vitreschak A.G., Mironov A.A., Gelfand M.S.;
RT "Comparative genomics of thiamin biosynthesis in procaryotes. New genes and
RT regulatory mechanisms.";
RL J. Biol. Chem. 277:48949-48959(2002).
RN [4]
RP FUNCTION IN HMP/THIAMINE TRANSPORT.
RC STRAIN=168 / PY79;
RX PubMed=16291685; DOI=10.1128/jb.187.23.8127-8136.2005;
RA Schyns G., Potot S., Geng Y., Barbosa T.M., Henriques A., Perkins J.B.;
RT "Isolation and characterization of new thiamine-deregulated mutants of
RT Bacillus subtilis.";
RL J. Bacteriol. 187:8127-8136(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH THIAMINE, AND
RP SUBUNIT.
RX PubMed=15451668; DOI=10.1016/j.jmb.2004.08.037;
RA Devedjiev Y., Surendranath Y., Derewenda U., Gabrys A., Cooper D.R.,
RA Zhang R.G., Lezondra L., Joachimiak A., Derewenda Z.S.;
RT "The structure and ligand binding properties of the B. subtilis YkoF gene
RT product, a member of a novel family of thiamin/HMP-binding proteins.";
RL J. Mol. Biol. 343:395-406(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "2.2-A crystal structure of protein ykoF from Bacillus subtilis.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Part of the ABC transporter complex YkoCDEF that could
CC transport hydroxymethylpyrimidine (HMP) and/or thiamine. Could also
CC transport other HMP-containing products. Binds thiamine via its HMP
CC moiety. {ECO:0000269|PubMed:12376536, ECO:0000269|PubMed:16291685}.
CC -!- SUBUNIT: Homodimer in vitro. In vivo, may be a part of an ABC
CC transporter complex which is composed of two ATP-binding proteins
CC (YkoD), two transmembrane proteins (YkoC and YkoE) and a solute-binding
CC protein (YkoF) (Probable). {ECO:0000305|PubMed:15451668,
CC ECO:0000305|Ref.6}.
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DR EMBL; AJ002571; CAA05603.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13181.1; -; Genomic_DNA.
DR PIR; B69859; B69859.
DR RefSeq; NP_389207.1; NC_000964.3.
DR RefSeq; WP_003244962.1; NZ_JNCM01000035.1.
DR PDB; 1S7H; X-ray; 2.20 A; A/B/C/D=1-200.
DR PDB; 1S99; X-ray; 1.65 A; A/B=1-200.
DR PDB; 1SBR; X-ray; 2.30 A; A/B=1-200.
DR PDBsum; 1S7H; -.
DR PDBsum; 1S99; -.
DR PDBsum; 1SBR; -.
DR AlphaFoldDB; O34911; -.
DR SMR; O34911; -.
DR STRING; 224308.BSU13240; -.
DR PaxDb; O34911; -.
DR PRIDE; O34911; -.
DR EnsemblBacteria; CAB13181; CAB13181; BSU_13240.
DR GeneID; 936465; -.
DR KEGG; bsu:BSU13240; -.
DR PATRIC; fig|224308.179.peg.1438; -.
DR eggNOG; ENOG502ZBT9; Bacteria.
DR OMA; CQFALYP; -.
DR BioCyc; BSUB:BSU13240-MON; -.
DR EvolutionaryTrace; O34911; -.
DR PRO; PR:O34911; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR Gene3D; 3.30.70.930; -; 2.
DR InterPro; IPR015835; HMP/thiamine-bd.
DR InterPro; IPR029756; MTH1187/YkoF-like.
DR InterPro; IPR011522; Thiamin/HMP-bd_put_YkoF.
DR Pfam; PF07615; Ykof; 2.
DR PIRSF; PIRSF021331; YkoF; 1.
DR SUPFAM; SSF89957; SSF89957; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transport.
FT CHAIN 1..200
FT /note="Putative HMP/thiamine-binding protein YkoF"
FT /id="PRO_0000288884"
FT BINDING 17
FT /ligand="thiamine"
FT /ligand_id="ChEBI:CHEBI:18385"
FT /evidence="ECO:0000269|PubMed:15451668"
FT BINDING 49
FT /ligand="thiamine"
FT /ligand_id="ChEBI:CHEBI:18385"
FT /evidence="ECO:0000269|PubMed:15451668"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:1S99"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1S99"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1S99"
FT TURN 103..110
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1S99"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1S99"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:1S99"
FT STRAND 179..190
FT /evidence="ECO:0007829|PDB:1S99"
SQ SEQUENCE 200 AA; 22024 MW; A75C6662174F9465 CRC64;
MEHICGTSRI AGFRFSLYPM TDDFISVIKS ALKKTDTSKV WTKTDHISTV LRGSIDHVFD
AAKAIYLHAA NSEQHIVMNG TFSIGCPGDT QGDTYLSKGD KRVNEDAVRG LKAEAPCQFA
LYPMNEPDYM GLIMEAVDIA KAQGTFVQGV HYASELDGDA HDVFSTLEAV FRMAEQQTNH
ITMTVNLSAN SPSRKNRKQG
