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YYDI_BACSU
ID   YYDI_BACSU              Reviewed;         209 AA.
AC   Q45593; Q794X2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable peptide export ATP-binding protein YydI;
GN   Name=yydI; OrderedLocusNames=BSU40150;
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;
RX   PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA   Kasahara Y., Nakai S., Ogasawara N.;
RT   "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT   Bacillus subtilis genome.";
RL   DNA Res. 4:155-159(1997).
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   TRANSCRIPTION REGULATION, AND OPERON SUGGESTION.
RC   STRAIN=168;
RX   PubMed=15743949; DOI=10.1128/jb.187.6.2010-2019.2005;
RA   Albano M., Smits W.K., Ho L.T., Kraigher B., Mandic-Mulec I., Kuipers O.P.,
RA   Dubnau D.;
RT   "The Rok protein of Bacillus subtilis represses genes for cell surface and
RT   extracellular functions.";
RL   J. Bacteriol. 187:2010-2019(2005).
RN   [4]
RP   SUGGESTION OF FUNCTION, OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=17921301; DOI=10.1128/jb.01181-07;
RA   Butcher B.G., Lin Y.-P., Helmann J.D.;
RT   "The yydFGHIJ operon of Bacillus subtilis encodes a peptide that induces
RT   the LiaRS two-component system.";
RL   J. Bacteriol. 189:8616-8625(2007).
CC   -!- FUNCTION: Suggested to be part of an ABC transporter complex YydIJ
CC       involved in export of the modified peptide YydF (Probable). Responsible
CC       for energy coupling to the transport system (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (YydI),
CC       two transmembrane proteins (YydJ). {ECO:0000305}.
CC   -!- INDUCTION: Transcriptionally repressed by rok (PubMed:15743949), this
CC       was not found to be the case in another study (PubMed:17921301).
CC       {ECO:0000269|PubMed:15743949, ECO:0000269|PubMed:17921301}.
CC   -!- DISRUPTION PHENOTYPE: Up-regulates expression of the LiaRS two-
CC       component regulatory system; this effect is more pronounced on modified
CC       competence medium than on rich or sporulation medium.
CC       {ECO:0000269|PubMed:17921301}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; D78193; BAA11273.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16052.1; -; Genomic_DNA.
DR   PIR; G70091; G70091.
DR   RefSeq; NP_391895.1; NC_000964.3.
DR   RefSeq; WP_003242913.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; Q45593; -.
DR   SMR; Q45593; -.
DR   STRING; 224308.BSU40150; -.
DR   TCDB; 3.A.1.133.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q45593; -.
DR   PRIDE; Q45593; -.
DR   EnsemblBacteria; CAB16052; CAB16052; BSU_40150.
DR   GeneID; 937743; -.
DR   KEGG; bsu:BSU40150; -.
DR   PATRIC; fig|224308.179.peg.4343; -.
DR   eggNOG; COG1131; Bacteria.
DR   OMA; MNIANYT; -.
DR   PhylomeDB; Q45593; -.
DR   BioCyc; BSUB:BSU40150-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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..209
FT                   /note="Probable peptide export ATP-binding protein YydI"
FT                   /id="PRO_0000370196"
FT   DOMAIN          1..207
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   209 AA;  23883 MW;  07BC160B3B3BE3A3 CRC64;
     MNIANYTLKV KGKTLLQDTD LHFSSGKINH VVGKNGVGKS QLAKDFLLNN SKRIGRDIRQ
     NVSLISSSSN IPNDVSKDFL LHFLSKKFDA KMIDKIAYLL NLDNIDGKVL IKNLSDGQKQ
     KLKLLSFLLE DKNIIVLDEI TNSLDKKTVI EIHGFLNKYI QENPEKIIIN ITHDLSDLKA
     IEGDYYIFNH QEIQQYHSVD KLIEVYINE
 
 
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