MCIZ_BACSU
ID MCIZ_BACSU Reviewed; 40 AA.
AC L8EBJ9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Cell division inhibitor MciZ {ECO:0000305};
DE AltName: Full=FtsZ assembly inhibitor {ECO:0000303|PubMed:23237472};
DE AltName: Full=Mother cell inhibitor of FtsZ {ECO:0000303|PubMed:18284588};
GN Name=mciZ {ECO:0000303|PubMed:18284588};
GN OrderedLocusNames=BSU_23616 {ECO:0000312|EMBL:CCQ48600.1};
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP IDENTIFICATION, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH FTSZ,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=168 / PY79;
RX PubMed=18284588; DOI=10.1111/j.1365-2958.2008.06173.x;
RA Handler A.A., Lim J.E., Losick R.;
RT "Peptide inhibitor of cytokinesis during sporulation in Bacillus
RT subtilis.";
RL Mol. Microbiol. 68:588-599(2008).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH FTSZ.
RX PubMed=23237472; DOI=10.1021/bi301237m;
RA Ray S., Kumar A., Panda D.;
RT "GTP regulates the interaction between MciZ and FtsZ: a possible role of
RT MciZ in bacterial cell division.";
RL Biochemistry 52:392-401(2013).
RN [4] {ECO:0007744|PDB:2MRW, ECO:0007744|PDB:4U39}
RP X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) IN COMPLEX WITH FTSZ, STRUCTURE BY
RP NMR, FUNCTION, SUBUNIT, INTERACTION WITH FTSZ, AND MUTAGENESIS OF ARG-20.
RC STRAIN=168 / PY79;
RX PubMed=25848052; DOI=10.1073/pnas.1414242112;
RA Bisson-Filho A.W., Discola K.F., Castellen P., Blasios V., Martins A.,
RA Sforca M.L., Garcia W., Zeri A.C., Erickson H.P., Dessen A.,
RA Gueiros-Filho F.J.;
RT "FtsZ filament capping by MciZ, a developmental regulator of bacterial
RT division.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E2130-E2138(2015).
CC -!- FUNCTION: Blocks Z-ring formation in the mother cell during sporulation
CC by inhibiting the polymerization of FtsZ (PubMed:18284588,
CC PubMed:23237472, PubMed:25848052). Binds to the minus end of FtsZ and
CC functions as a filament-capping protein (PubMed:25848052). At high
CC concentrations, is capable of both capping and sequestration of FtsZ
CC (PubMed:25848052). Decreases the GTPase activity of FtsZ
CC (PubMed:18284588, PubMed:23237472, PubMed:25848052).
CC {ECO:0000269|PubMed:18284588, ECO:0000269|PubMed:23237472,
CC ECO:0000269|PubMed:25848052}.
CC -!- ACTIVITY REGULATION: Highly effective in inhibiting polymerization at
CC low and intermediate concentrations of GTP and only partially effective
CC at high GTP concentrations. {ECO:0000269|PubMed:18284588,
CC ECO:0000269|PubMed:23237472}.
CC -!- SUBUNIT: Interacts with FtsZ (PubMed:18284588, PubMed:23237472,
CC PubMed:25848052). Binds to the C-terminal polymerization interface of
CC FtsZ (PubMed:25848052). Binds to FtsZ filaments (PubMed:25848052).
CC {ECO:0000269|PubMed:18284588, ECO:0000269|PubMed:23237472,
CC ECO:0000269|PubMed:25848052}.
CC -!- DEVELOPMENTAL STAGE: Expressed at an intermediate stage of sporulation.
CC {ECO:0000269|PubMed:18284588}.
CC -!- INDUCTION: Expression is regulated by the mother cell-specific factor
CC sigma E. {ECO:0000269|PubMed:18284588}.
CC -!- CAUTION: Ray et al suggested that MciZ competes with GTP for binding to
CC FtsZ, but Bisson-Filho et al showed later that MciZ and GTP bind at
CC opposite surfaces of FtsZ, and that MciZ does not compete with GTP
CC binding. {ECO:0000305|PubMed:23237472, ECO:0000305|PubMed:25848052}.
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DR EMBL; AL009126; CCQ48600.1; -; Genomic_DNA.
DR RefSeq; WP_003230420.1; NZ_JNCM01000036.1.
DR PDB; 2MRW; NMR; -; A=1-40.
DR PDB; 4U39; X-ray; 3.19 A; J/K/L/M/N/O/P/Q/R=1-40.
DR PDBsum; 2MRW; -.
DR PDBsum; 4U39; -.
DR AlphaFoldDB; L8EBJ9; -.
DR SMR; L8EBJ9; -.
DR STRING; 224308.BSU23616; -.
DR PaxDb; L8EBJ9; -.
DR EnsemblBacteria; CCQ48600; CCQ48600; BSU_23616.
DR PATRIC; fig|224308.179.peg.2574; -.
DR BioCyc; BSUB:MON8J2-50; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR025177; MciZ.
DR Pfam; PF13072; MciZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Sporulation.
FT CHAIN 1..40
FT /note="Cell division inhibitor MciZ"
FT /id="PRO_0000444620"
FT MUTAGEN 20
FT /note="R->D: Disrupts interaction with FtsZ."
FT /evidence="ECO:0000269|PubMed:25848052"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4U39"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4U39"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:4U39"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:4U39"
SQ SEQUENCE 40 AA; 4775 MW; 0B3278122AEB7135 CRC64;
MKVHRMPKGV VLVGKAWEIR AKLKEYGRTF QYVKDWISKP
