ID   MINC_RALPJ              Reviewed;         264 AA.
AC   B2UGZ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Rpic_3561;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001068; ACD28680.1; -; Genomic_DNA.
DR   RefSeq; WP_012436753.1; NC_010682.1.
DR   AlphaFoldDB; B2UGZ7; -.
DR   SMR; B2UGZ7; -.
DR   STRING; 402626.Rpic_3561; -.
DR   EnsemblBacteria; ACD28680; ACD28680; Rpic_3561.
DR   KEGG; rpi:Rpic_3561; -.
DR   PATRIC; fig|402626.5.peg.4699; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_067812_0_0_4; -.
DR   OMA; RRDPLWG; -.
DR   OrthoDB; 1665744at2; -.
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; Septation.
FT   CHAIN           1..264
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000114286"
FT   REGION          103..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  28386 MW;  87A9B6C20582C63C CRC64;
     MSQKKAPLFE IRSGTVDALL LSPRTADMDA LAAELTRRFA DTPEFFSNDV IAIDVRRLAE
     DERLPIDRLV ETLTALRARA IGVVASPEQA GWAQAFGLPL LDSHGRRPRG GNDAKDADRN
     DAQDAQGAPE HAQAAEAPAS TSAIPPADAA AMQPGTMIVD RPLRSGQRIY ARGDLVVLDL
     VSDGAEVIAE GNIYVYASLR GRALAGVKGN LDARIFCTCL EPQLISIAGI YRTGETPWPD
     AYASKPAQVR LADNTLVFEP LRMK