YKOE_BACSU
ID YKOE_BACSU Reviewed; 199 AA.
AC O34738; Q796L8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Putative HMP/thiamine permease protein YkoE;
GN Name=ykoE; OrderedLocusNames=BSU13230;
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 SEQUENCE REVISION TO 169.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
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 [5]
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).
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. Probably responsible for the
CC translocation of the substrate across the membrane (Probable).
CC {ECO:0000305|PubMed:12376536, ECO:0000305|PubMed:16291685}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (YkoD),
CC two transmembrane proteins (YkoC and YkoE) and a solute-binding protein
CC (YkoF). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AJ002571; CAA05602.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13180.2; -; Genomic_DNA.
DR PIR; A69859; A69859.
DR RefSeq; NP_389206.2; NC_000964.3.
DR RefSeq; WP_003232554.1; NZ_JNCM01000035.1.
DR PDB; 5EDL; X-ray; 1.95 A; A=3-199.
DR PDBsum; 5EDL; -.
DR AlphaFoldDB; O34738; -.
DR SMR; O34738; -.
DR STRING; 224308.BSU13230; -.
DR TCDB; 3.A.1.30.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34738; -.
DR EnsemblBacteria; CAB13180; CAB13180; BSU_13230.
DR GeneID; 939829; -.
DR KEGG; bsu:BSU13230; -.
DR PATRIC; fig|224308.179.peg.1437; -.
DR eggNOG; COG4721; Bacteria.
DR OMA; GVIFWAW; -.
DR PhylomeDB; O34738; -.
DR BioCyc; BSUB:BSU13230-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR017195; ABC_thiamin-permease_prd.
DR Pfam; PF09819; ABC_cobalt; 1.
DR PIRSF; PIRSF037394; ABC_thiamine-permease_YkoE_prd; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..199
FT /note="Putative HMP/thiamine permease protein YkoE"
FT /id="PRO_0000289023"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 169
FT /note="D -> G (in Ref. 1; CAA05602)"
FT /evidence="ECO:0000305"
FT HELIX 6..37
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:5EDL"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 87..105
FT /evidence="ECO:0007829|PDB:5EDL"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 113..134
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:5EDL"
FT TURN 173..179
FT /evidence="ECO:0007829|PDB:5EDL"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:5EDL"
SQ SEQUENCE 199 AA; 21224 MW; 2709E2C5A7A1F31F CRC64;
MKSWKVKEIV IMSVISIVFA VVYLLFTHFG NVLAGMFGPI AYEPIYGIWF IVSVIAAYMI
RKPGAALVSE IIAALVECLL GNPSGPMVIV IGIVQGLGAE AVFLATRWKA YSLPVLMLAG
MGSSVASFIY DLFVSGYAAY SPGYLLIMLV IRLISGALLA GLLGKAVSDS LAYTGVLNGM
ALGKELKKKR KRASEHASL
