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MINJ_BACSU
ID   MINJ_BACSU              Reviewed;         397 AA.
AC   O34375; Q795D8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cell division topological determinant MinJ;
GN   Name=minJ; Synonyms=swrAB, yvjD; OrderedLocusNames=BSU35220;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT   subtilis.";
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   PRELIMINARY FUNCTION.
RX   PubMed=16030230; DOI=10.1128/jb.187.15.5356-5366.2005;
RA   Calvio C., Celandroni F., Ghelardi E., Amati G., Salvetti S., Ceciliani F.,
RA   Galizzi A., Senesi S.;
RT   "Swarming differentiation and swimming motility in Bacillus subtilis are
RT   controlled by swrA, a newly identified dicistronic operon.";
RL   J. Bacteriol. 187:5356-5366(2005).
RN   [4]
RP   FUNCTION, INTERACTION WITH DIVIVA AND MIND, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=3610;
RX   PubMed=18976281; DOI=10.1111/j.1365-2958.2008.06469.x;
RA   Patrick J.E., Kearns D.B.;
RT   "MinJ (YvjD) is a topological determinant of cell division in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 70:1166-1179(2008).
RN   [5]
RP   FUNCTION, INTERACTION WITH DIVIVA AND MIND, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=19019154; DOI=10.1111/j.1365-2958.2008.06501.x;
RA   Bramkamp M., Emmins R., Weston L., Donovan C., Daniel R.A., Errington J.;
RT   "A novel component of the division-site selection system of Bacillus
RT   subtilis and a new mode of action for the division inhibitor MinCD.";
RL   Mol. Microbiol. 70:1556-1569(2008).
RN   [6]
RP   FUNCTION OF THE MIN SYSTEM, AND SUBCELLULAR LOCATION.
RX   PubMed=20352045; DOI=10.1371/journal.pone.0009850;
RA   van Baarle S., Bramkamp M.;
RT   "The MinCDJ system in Bacillus subtilis prevents minicell formation by
RT   promoting divisome disassembly.";
RL   PLoS ONE 5:E9850-E9850(2010).
CC   -!- FUNCTION: The main function of the Min system is to promote the
CC       disassembly of the cytokinetic ring after cell division, thereby
CC       ensuring that division occurs only once per cell cycle. MinJ acts as a
CC       bridge between DivIVA and MinD. May modulate activity and localization
CC       of MinD and MinC through direct interaction with MinD.
CC       {ECO:0000269|PubMed:18976281, ECO:0000269|PubMed:19019154,
CC       ECO:0000269|PubMed:20352045}.
CC   -!- SUBUNIT: Interacts directly with DivIVA and MinD.
CC       {ECO:0000269|PubMed:18976281, ECO:0000269|PubMed:19019154}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18976281,
CC       ECO:0000269|PubMed:19019154, ECO:0000269|PubMed:20352045}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:18976281,
CC       ECO:0000269|PubMed:19019154, ECO:0000269|PubMed:20352045}.
CC       Note=Localization depends on DivIVA and on the state of the cell cycle.
CC       Present at both cell poles in non-dividing cells. As cells prepare to
CC       divide, moves from poles to mid-cell. Then, after division is
CC       completed, stays associated with new poles, but also moves back to old
CC       poles.
CC   -!- DISRUPTION PHENOTYPE: Mutants show defects in homologous recombination,
CC       swarming motility and cell division. {ECO:0000269|PubMed:18976281,
CC       ECO:0000269|PubMed:19019154}.
CC   -!- SIMILARITY: Belongs to the MinJ family. {ECO:0000305}.
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DR   EMBL; AF017113; AAC67265.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15539.1; -; Genomic_DNA.
DR   PIR; F70042; F70042.
DR   RefSeq; NP_391402.1; NC_000964.3.
DR   RefSeq; WP_003242631.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O34375; -.
DR   SMR; O34375; -.
DR   STRING; 224308.BSU35220; -.
DR   PaxDb; O34375; -.
DR   EnsemblBacteria; CAB15539; CAB15539; BSU_35220.
DR   GeneID; 936668; -.
DR   KEGG; bsu:BSU35220; -.
DR   PATRIC; fig|224308.179.peg.3812; -.
DR   eggNOG; COG0265; Bacteria.
DR   OMA; EHHELGI; -.
DR   PhylomeDB; O34375; -.
DR   BioCyc; BSUB:BSU35220-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   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   Pfam; PF17820; PDZ_6; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome;
KW   Septation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..397
FT                   /note="Cell division topological determinant MinJ"
FT                   /id="PRO_0000360825"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          279..363
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
SQ   SEQUENCE   397 AA;  43666 MW;  2959596C5D1962C2 CRC64;
     MSVQWGIELL KSAGLFFLHP LFWFFIIITL AFGYVRIKRE RKTFHTRIAD IYDDLKFTYT
     KGLIPGLLLS VILGGLGISI PLGLLAIIAV ITAAAAFTLR ANWMSAAYIV SVSMLIGFGL
     QIYQAEPFLE RFPQGFAVVW PAVAVFLGLL IITEGAVAYR SAHVRTSPAL VVSSRGLPIG
     QQLANRVWLL PLFLLVPGNG LESHLSWWPV FTVPGGSFHF LWIPYFVGFG QRVQGSLPET
     SIRITAKRVC ILGLAVAVLG AASLLWTPLA GAAVCTALLG RIFLSIKQRV NDNAAPFYFS
     KRDQGLMVLG IIPNTPAEDL ELKIGEIITK VNGIPVKNVS DFYEALQHNR AYVKLEIIGL
     NGEIRFDQRA SYEGEHHELG ILFVKDDRED EAVASGS
 
 
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