ID   MINC_XANC8              Reviewed;         249 AA.
AC   Q4US07;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=XC_3121;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY50166.1; -; Genomic_DNA.
DR   RefSeq; WP_011269938.1; NC_007086.1.
DR   AlphaFoldDB; Q4US07; -.
DR   SMR; Q4US07; -.
DR   EnsemblBacteria; AAY50166; AAY50166; XC_3121.
DR   KEGG; xcb:XC_3121; -.
DR   HOGENOM; CLU_067812_0_1_6; -.
DR   OMA; RRDPLWG; -.
DR   OrthoDB; 1665744at2; -.
DR   Proteomes; UP000000420; 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; Septation.
FT   CHAIN           1..249
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000047875"
FT   REGION          117..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..133
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  26676 MW;  8EFC0E24E0C27F94 CRC64;
     MSSVNVDFEQ AGELKIGQVG IANLRIRTLD VPRLVREMQD RVTRAPKLFG RAAVILDFGG
     LAQAPDLATA KALLDGLRSA GVLPVALAYG TSEIDLLSQQ LGIPLLAKFR AQYETAAVRP
     PQPPPPPHAR AEPAAPVARP APVRMQRNTV RSGQQLYAEN CDLTVLSTVG AGAEVIADGS
     IHIYGTLRGR ALAGAQGNPD ARIFCRDFHA ELVAIAGHYK VLDDVPMDLR GKAVQVWLEQ
     DQIKIAALD