YKOD_BACSU
ID YKOD_BACSU Reviewed; 547 AA.
AC O34362; Q796L9;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative HMP/thiamine import ATP-binding protein YkoD;
DE EC=7.6.2.-;
GN Name=ykoD; OrderedLocusNames=BSU13220;
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 134 AND C-TERMINUS.
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. Responsible for energy
CC coupling to the transport system (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:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05601.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ002571; CAA05601.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB13179.2; -; Genomic_DNA.
DR PIR; H69858; H69858.
DR RefSeq; NP_389205.2; NC_000964.3.
DR RefSeq; WP_003245821.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34362; -.
DR SMR; O34362; -.
DR STRING; 224308.BSU13220; -.
DR TCDB; 3.A.1.30.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34362; -.
DR PRIDE; O34362; -.
DR EnsemblBacteria; CAB13179; CAB13179; BSU_13220.
DR GeneID; 936472; -.
DR KEGG; bsu:BSU13220; -.
DR PATRIC; fig|224308.179.peg.1436; -.
DR eggNOG; COG1122; Bacteria.
DR InParanoid; O34362; -.
DR OMA; MYRGEQV; -.
DR PhylomeDB; O34362; -.
DR BioCyc; BSUB:BSU13220-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..547
FT /note="Putative HMP/thiamine import ATP-binding protein
FT YkoD"
FT /id="PRO_0000091988"
FT DOMAIN 8..250
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 295..523
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 327..334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 134
FT /note="E -> G (in Ref. 1; CAA05601)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="L -> Q (in Ref. 1; CAA05601)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="G -> A (in Ref. 1; CAA05601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 61146 MW; E99FF0F26503505E CRC64;
MQAFDELLTV EQLSFSYEED EKPVFQDISF ELQKGECVLL LGPSGCGKSS LALCLNGLYP
EACDGIQSGH VFLFQKPVTD AETSETITQH AGVVFQDPDQ QFCMLTVEDE IAFGLENLQI
PKEEMTEKIN AVLEKLRITH LKEKMISTLS GGQKQKVALA CILAMEPELI ILDEPTSLLD
PFSAREFVHL MKDLQREKGF SLLVIEHQLD EWAPWIERTI VLDKSGKKAL DGLTKNLFQH
EAETLKKLGI AIPKVCHLQE KLSMPFTLSK EMLFKEPIPA GHVKKKKAPS GESVLEVSSL
SFARGQQAIF KDISFSLREG SLTALVGPNG TGKSTLLSVL ASLMKPQSGK ILLYDQPLQK
YKEKELRKRM GFVFQNPEHQ FVTDTVYDEL LFGQKANAET EKKAQHLLQR FGLAHLADHH
PFAISQGQKR RLSVATMLMH DVKVLLLDEP TFGQDARTAA ECMEMIQRIK AEGTAVLMIT
HDMELVSSYA DSVLVLHDTG LAFDGSPAQL FSQETGLVQK AKLTLPLLYE WMAFQEEVRD
EATVTSH
