ID   MINC_RALSO              Reviewed;         255 AA.
AC   Q8XU30;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=RSc3364;
GN   ORFNames=RS02639;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646052; CAD16861.1; -; Genomic_DNA.
DR   RefSeq; WP_011003246.1; NC_003295.1.
DR   AlphaFoldDB; Q8XU30; -.
DR   SMR; Q8XU30; -.
DR   STRING; 267608.RSc3364; -.
DR   EnsemblBacteria; CAD16861; CAD16861; RSc3364.
DR   GeneID; 60502876; -.
DR   KEGG; rso:RSc3364; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_067812_0_0_4; -.
DR   OMA; RRDPLWG; -.
DR   Proteomes; UP000001436; 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..255
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_0000189057"
FT   REGION          103..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   255 AA;  27400 MW;  29D63BB04595371A CRC64;
     MSQKKAPLFE IRSGTVDALL LSPRTADMDA LAAELTRRFA DTPEFFSNDV IAIDVRRLAA
     DERLPIDRLV ETLTGLRARA IGVVASPEQA EWAQACGLPL LDSHGRRPRG ERSEEAAEAV
     PAAAEPVPAP AASPAPPVEA VAMQPGAMII EKPLRSGQRV YARGDLVVLD LVSDGAEVIA
     EGNIYVYASL RGRALAGVKG NLDARIFCTC LEPQLISIAG IYRTGETPWP EAFASKPAQI
     RLSENTLVLE PLRMK