ID   MINC_CUPMC              Reviewed;         282 AA.
AC   Q1LSF5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Probable septum site-determining protein MinC {ECO:0000255|HAMAP-Rule:MF_00267};
GN   Name=minC {ECO:0000255|HAMAP-Rule:MF_00267}; OrderedLocusNames=Rmet_0035;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SIMILARITY: Belongs to the MinC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
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DR   EMBL; CP000352; ABF06921.1; -; Genomic_DNA.
DR   RefSeq; WP_011514963.1; NC_007973.1.
DR   AlphaFoldDB; Q1LSF5; -.
DR   SMR; Q1LSF5; -.
DR   STRING; 266264.Rmet_0035; -.
DR   EnsemblBacteria; ABF06921; ABF06921; Rmet_0035.
DR   KEGG; rme:Rmet_0035; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_067812_0_0_4; -.
DR   OrthoDB; 1665744at2; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
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; IPR007874; MinC_N.
DR   InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR   PANTHER; PTHR34108; PTHR34108; 1.
DR   Pfam; PF03775; MinC_C; 1.
DR   Pfam; PF05209; MinC_N; 1.
DR   SUPFAM; SSF63848; SSF63848; 1.
DR   TIGRFAMs; TIGR01222; minC; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Reference proteome; Septation.
FT   CHAIN           1..282
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000047850"
FT   REGION          103..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  29772 MW;  310E160AEF56F6A5 CRC64;
     MSQKKSPRFE LRSGNVDALL LALNTADLDA VRDDLLSRFE STPDFFSDDV VALDLRRLEG
     TGALALDRVI DTLATLKARA IGVVARADQR DWAGGFGLPL LDSQSRRGGK DEAPKEKAGK
     PEATAASGQT DAEAAGNTGK GKDSEGAAVN GKASEIAEIM AAANAASAPR AIPTLLIDKP
     LRSGQQIYAQ GDVVILDLVS YGAEVIAEGN IHIYAPLRGR ALAGVKGNPD ARIFCTCLEP
     ELISIAGIYR TAEQTLPADV LGKSAQVRLA DEKLILEPLR MK