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MINC_BACSU
ID   MINC_BACSU              Reviewed;         226 AA.
AC   Q01463;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Septum site-determining protein MinC;
GN   Name=minC; OrderedLocusNames=BSU28000;
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=1400225; DOI=10.1128/jb.174.21.6729-6742.1992;
RA   Varley A.W., Stewart G.C.;
RT   "The divIVB region of the Bacillus subtilis chromosome encodes homologs of
RT   Escherichia coli septum placement (minCD) and cell shape (mreBCD)
RT   determinants.";
RL   J. Bacteriol. 174:6729-6742(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8459776; DOI=10.1111/j.1365-2958.1993.tb01151.x;
RA   Lee S., Price C.W.;
RT   "The minCD locus of Bacillus subtilis lacks the minE determinant that
RT   provides topological specificity to cell division.";
RL   Mol. Microbiol. 7:601-610(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1400224; DOI=10.1128/jb.174.21.6717-6728.1992;
RA   Levin P.A., Margolis P.S., Setlow P., Losick R., Sun D.;
RT   "Identification of Bacillus subtilis genes for septum placement and shape
RT   determination.";
RL   J. Bacteriol. 174:6717-6728(1992).
RN   [4]
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=9765563; DOI=10.1128/jb.180.20.5327-5333.1998;
RA   Barak I., Prepiak P., Schmeisser F.;
RT   "MinCD proteins control the septation process during sporulation of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 180:5327-5333(1998).
CC   -!- FUNCTION: Cell division inhibitor that blocks the formation of polar Z
CC       ring septums. Rapidly oscillates between the poles of the cell to
CC       destabilize FtsZ filaments that have formed before they mature into
CC       polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an
CC       important role in asymmetric septum formation during sporulation of
CC       B.subtilis cells.
CC   -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q01463; Q01464: minD; NbExp=3; IntAct=EBI-9304968, EBI-6502875;
CC   -!- SIMILARITY: Belongs to the MinC family. {ECO:0000305}.
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DR   EMBL; M95582; AAA22608.1; -; Genomic_DNA.
DR   EMBL; Z15113; CAA78817.1; -; Genomic_DNA.
DR   EMBL; M96343; AAA22400.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14760.1; -; Genomic_DNA.
DR   PIR; S31204; F45239.
DR   RefSeq; NP_390678.1; NC_000964.3.
DR   RefSeq; WP_004398901.1; NZ_JNCM01000036.1.
DR   PDB; 2M4I; NMR; -; A=1-102.
DR   PDBsum; 2M4I; -.
DR   AlphaFoldDB; Q01463; -.
DR   BMRB; Q01463; -.
DR   SMR; Q01463; -.
DR   IntAct; Q01463; 2.
DR   STRING; 224308.BSU28000; -.
DR   PaxDb; Q01463; -.
DR   PRIDE; Q01463; -.
DR   DNASU; 937500; -.
DR   EnsemblBacteria; CAB14760; CAB14760; BSU_28000.
DR   GeneID; 937500; -.
DR   KEGG; bsu:BSU28000; -.
DR   PATRIC; fig|224308.179.peg.3042; -.
DR   eggNOG; COG0850; Bacteria.
DR   InParanoid; Q01463; -.
DR   OMA; EMECAYI; -.
DR   PhylomeDB; Q01463; -.
DR   BioCyc; BSUB:BSU28000-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0032272; P:negative regulation of protein polymerization; IDA:CACAO.
DR   GO; GO:1901891; P:regulation of cell septum assembly; IEA:InterPro.
DR   Gene3D; 2.160.20.70; -; 1.
DR   HAMAP; MF_00267; MinC; 1.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR013033; MinC.
DR   InterPro; IPR036145; MinC_C_sf.
DR   InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR   PANTHER; PTHR34108; PTHR34108; 1.
DR   Pfam; PF03775; MinC_C; 1.
DR   SUPFAM; SSF63848; SSF63848; 1.
DR   TIGRFAMs; TIGR01222; minC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Reference proteome; Septation.
FT   CHAIN           1..226
FT                   /note="Septum site-determining protein MinC"
FT                   /id="PRO_0000189017"
FT   STRAND          9..12
FT                   /evidence="ECO:0007829|PDB:2M4I"
FT   STRAND          14..22
FT                   /evidence="ECO:0007829|PDB:2M4I"
FT   HELIX           30..42
FT                   /evidence="ECO:0007829|PDB:2M4I"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:2M4I"
FT   HELIX           65..76
FT                   /evidence="ECO:0007829|PDB:2M4I"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:2M4I"
SQ   SEQUENCE   226 AA;  24998 MW;  25C8F1503F89BF60 CRC64;
     MKTKKQQYVT IKGTKNGLTL HLDDACSFDE LLDGLQNMLS IEQYTDGKGQ KISVHVKLGN
     RFLYKEQEEQ LTELIASKKD LFVHSIDSEV ITKKEAQQIR EEAEIISVSK IVRSGQVLQV
     KGDLLLIGDV NPGGTVRAGG NIFVLGSLKG IAHAGFNGNN QAVIAASEML PTQLRINHVL
     NRSPDHIQKG NEMECAYLDT DGNMVIERLQ HLAHLRPDLT RLEGGM
 
 
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