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DIV4A_BACSU
ID   DIV4A_BACSU             Reviewed;         164 AA.
AC   P71021; O08052; Q796I7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Septum site-determining protein DivIVA;
DE   AltName: Full=Cell division initiation protein DivIVA;
DE   AltName: Full=Minicell-associated protein DivIVA;
GN   Name=divIVA; Synonyms=ylmJ; OrderedLocusNames=BSU15420;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ALA-78 AND
RP   157-ASP--GLU-164, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=9045828; DOI=10.1128/jb.179.5.1671-1683.1997;
RA   Cha J.-H., Stewart G.C.;
RT   "The divIVA minicell locus of Bacillus subtilis.";
RL   J. Bacteriol. 179:1671-1683(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=9219999; DOI=10.1046/j.1365-2958.1997.3811764.x;
RA   Edwards D.H., Errington J.;
RT   "The Bacillus subtilis DivIVA protein targets to the division septum and
RT   controls the site specificity of cell division.";
RL   Mol. Microbiol. 24:905-915(1997).
RN   [3]
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   [4]
RP   MUTAGENESIS OF PHE-17; ARG-18; GLY-19 AND TYR-20.
RX   PubMed=15554965; DOI=10.1111/j.1365-2958.2004.04363.x;
RA   Perry S.E., Edwards D.H.;
RT   "Identification of a polar targeting determinant for Bacillus subtilis
RT   DivIVA.";
RL   Mol. Microbiol. 54:1237-1249(2004).
RN   [5]
RP   SUBUNIT, AND MUTAGENESIS OF LEU-121 AND GLU-162.
RX   PubMed=11882716; DOI=10.1099/00221287-148-3-807;
RA   Muchova K., Kutejova E., Scott D.J., Brannigan J.A., Lewis R.J.,
RA   Wilkinson A.J., Barak I.;
RT   "Oligomerization of the Bacillus subtilis division protein DivIVA.";
RL   Microbiology 148:807-813(2002).
RN   [6]
RP   SUBUNIT.
RX   PubMed=15165232; DOI=10.1111/j.1365-2958.2004.04074.x;
RA   Stahlberg H., Kutejova E., Muchova K., Gregorini M., Lustig A.,
RA   Mueller S.A., Olivieri V., Engel A., Wilkinson A.J., Barak I.;
RT   "Oligomeric structure of the Bacillus subtilis cell division protein DivIVA
RT   determined by transmission electron microscopy.";
RL   Mol. Microbiol. 52:1281-1290(2004).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH FTSZ; MIND AND SPO0J.
RX   PubMed=16885474; DOI=10.1128/jb.01750-05;
RA   Perry S.E., Edwards D.H.;
RT   "The Bacillus subtilis DivIVA protein has a sporulation-specific proximity
RT   to Spo0J.";
RL   J. Bacteriol. 188:6039-6043(2006).
RN   [8]
RP   INTERACTION WITH MINJ.
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   [9]
RP   INTERACTION WITH MINJ.
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).
CC   -!- FUNCTION: May act as a pilot protein, directing MinCD to the polar
CC       septation sites or by inhibiting MinCD at the midcell site of division.
CC       Required for polar localization of the chromosome during sporulation.
CC       {ECO:0000269|PubMed:9045828, ECO:0000269|PubMed:9219999}.
CC   -!- SUBUNIT: Oligomers. Interacts with FtsZ, MinD, MinJ and Spo0J. The
CC       association with Spo0J is transient and occurs at a specific point
CC       during development. {ECO:0000269|PubMed:11882716,
CC       ECO:0000269|PubMed:15165232, ECO:0000269|PubMed:16885474,
CC       ECO:0000269|PubMed:18976281, ECO:0000269|PubMed:19019154}.
CC   -!- INTERACTION:
CC       P71021; O32049: comN; NbExp=4; IntAct=EBI-5243654, EBI-6418652;
CC       P71021; P71021: divIVA; NbExp=10; IntAct=EBI-5243654, EBI-5243654;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16885474,
CC       ECO:0000269|PubMed:9219999}. Note=Localized at the cell division site
CC       and found exclusively at the cell pole during sporulation.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:9219999}.
CC   -!- DISRUPTION PHENOTYPE: Misplacement of the septum during cell division,
CC       resulting in the formation of small, circular, anucleate minicells.
CC       {ECO:0000269|PubMed:9045828, ECO:0000269|PubMed:9219999}.
CC   -!- MISCELLANEOUS: Overexpression of DivIVA is lethal.
CC   -!- SIMILARITY: Belongs to the DivIVA family. {ECO:0000305}.
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DR   EMBL; U60901; AAB49279.1; -; Genomic_DNA.
DR   EMBL; Z86114; CAB06818.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13416.1; -; Genomic_DNA.
DR   PIR; B69616; B69616.
DR   RefSeq; NP_389425.1; NC_000964.3.
DR   RefSeq; WP_003221468.1; NZ_JNCM01000035.1.
DR   PDB; 2WUJ; X-ray; 1.40 A; A/B=1-57.
DR   PDB; 2WUK; X-ray; 1.90 A; A/B/C/D=1-57.
DR   PDBsum; 2WUJ; -.
DR   PDBsum; 2WUK; -.
DR   AlphaFoldDB; P71021; -.
DR   SMR; P71021; -.
DR   IntAct; P71021; 11.
DR   MINT; P71021; -.
DR   STRING; 224308.BSU15420; -.
DR   jPOST; P71021; -.
DR   PaxDb; P71021; -.
DR   PRIDE; P71021; -.
DR   EnsemblBacteria; CAB13416; CAB13416; BSU_15420.
DR   GeneID; 64303433; -.
DR   GeneID; 939972; -.
DR   KEGG; bsu:BSU15420; -.
DR   PATRIC; fig|224308.179.peg.1680; -.
DR   eggNOG; COG3599; Bacteria.
DR   InParanoid; P71021; -.
DR   OMA; QSIFVAQ; -.
DR   PhylomeDB; P71021; -.
DR   BioCyc; BSUB:BSU15420-MON; -.
DR   EvolutionaryTrace; P71021; -.
DR   PRO; PR:P71021; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR019933; DivIVA_domain.
DR   InterPro; IPR007793; DivIVA_fam.
DR   PANTHER; PTHR35794; PTHR35794; 1.
DR   Pfam; PF05103; DivIVA; 1.
DR   TIGRFAMs; TIGR03544; DivI1A_domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Reference proteome; Septation; Sporulation.
FT   CHAIN           1..164
FT                   /note="Septum site-determining protein DivIVA"
FT                   /id="PRO_0000360608"
FT   COILED          29..107
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         17
FT                   /note="F->L: Diffuse localization."
FT                   /evidence="ECO:0000269|PubMed:15554965"
FT   MUTAGEN         18
FT                   /note="R->A,C: Localization at cytoplasmic foci instead of
FT                   the cell pole. Stable interaction with Spo0J and
FT                   association with the chromosome."
FT                   /evidence="ECO:0000269|PubMed:15554965"
FT   MUTAGEN         19
FT                   /note="G->A: Localized at cytoplasmic foci."
FT                   /evidence="ECO:0000269|PubMed:15554965"
FT   MUTAGEN         20
FT                   /note="Y->C: No effect on localization."
FT                   /evidence="ECO:0000269|PubMed:15554965"
FT   MUTAGEN         78
FT                   /note="A->T: In divIVA1; loss of function resulting in
FT                   sporulation defect and in the formation of minicells."
FT                   /evidence="ECO:0000269|PubMed:9045828"
FT   MUTAGEN         121
FT                   /note="L->P: In divIVA2; loss of function."
FT                   /evidence="ECO:0000269|PubMed:11882716"
FT   MUTAGEN         157..164
FT                   /note="DAVFEEKE->LQVSGVVI: No effect."
FT                   /evidence="ECO:0000269|PubMed:9045828"
FT   MUTAGEN         162
FT                   /note="E->K: No effect."
FT                   /evidence="ECO:0000269|PubMed:11882716"
FT   HELIX           5..8
FT                   /evidence="ECO:0007829|PDB:2WUJ"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:2WUJ"
FT   HELIX           22..51
FT                   /evidence="ECO:0007829|PDB:2WUJ"
SQ   SEQUENCE   164 AA;  19341 MW;  B62978CA02708F68 CRC64;
     MPLTPNDIHN KTFTKSFRGY DEDEVNEFLA QVRKDYEIVL RKKTELEAKV NELDERIGHF
     ANIEETLNKS ILVAQEAAED VKRNSQKEAK LIVREAEKNA DRIINESLSK SRKIAMEIEE
     LKKQSKVFRT RFQMLIEAQL DLLKNDDWDH LLEYEVDAVF EEKE
 
 
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