ID   MINC_BURM9              Reviewed;         270 AA.
AC   A2S9G8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable septum site-determining protein MinC {ECO:0000255|HAMAP-Rule:MF_00267};
GN   Name=minC {ECO:0000255|HAMAP-Rule:MF_00267};
GN   OrderedLocusNames=BMA10229_A2631;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(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; CP000546; ABN02141.1; -; Genomic_DNA.
DR   RefSeq; WP_004186698.1; NC_008836.1.
DR   AlphaFoldDB; A2S9G8; -.
DR   SMR; A2S9G8; -.
DR   EnsemblBacteria; ABN02141; ABN02141; BMA10229_A2631.
DR   GeneID; 56594880; -.
DR   KEGG; bml:BMA10229_A2631; -.
DR   HOGENOM; CLU_067812_0_0_4; -.
DR   OMA; RRDPLWG; -.
DR   Proteomes; UP000002283; Chromosome I.
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..270
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000047811"
FT   REGION          105..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  28940 MW;  40EE54AD4E1EDCF8 CRC64;
     MSLKKSPFFE LRSGSVDTLL FIVKTADLDA LRAELVKRFE ATPEFFADDV VAIDVRRLAD
     HERVPLDDIR GMLNDVRMRV IGVVAQPEQH AWAASAGLPL LEARDRRAPS SKAADEAPVQ
     QAEPAAPAAG QAALFEQAGP TLADAGAPPE SPAPAVAAQS ATLVVDRPLH SGQQIYAKGD
     LVVLGPVSYG AEVIAEGNIH IYAPLRGRAL AGVHGNHDAR IFCTCLEPEL ISIAGIYRTT
     ENPLPADVLG KSVQIRLEQE KLMIEPLRLT