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MINC_ECOL6
ID   MINC_ECOL6              Reviewed;         231 AA.
AC   Q8FI31;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Septum site-determining protein MinC;
GN   Name=minC {ECO:0000255|HAMAP-Rule:MF_00267}; OrderedLocusNames=c1623;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80088.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN80088.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000072533.1; NC_004431.1.
DR   AlphaFoldDB; Q8FI31; -.
DR   SMR; Q8FI31; -.
DR   STRING; 199310.c1623; -.
DR   EnsemblBacteria; AAN80088; AAN80088; c1623.
DR   KEGG; ecc:c1623; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_067812_0_1_6; -.
DR   OMA; RRDPLWG; -.
DR   Proteomes; UP000001410; 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..231
FT                   /note="Septum site-determining protein MinC"
FT                   /id="PRO_0000189034"
FT   REGION          102..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  24701 MW;  985D2CB76E8D7BC4 CRC64;
     MSNTPIELKG SSFTLSVVHL HEAEPKVIHQ ALEDKIAQAP AFLKHAPVVL NVSALEAPVN
     WSAMHKAVSA TGLRVIGVSG CKDAQLKAEI EKMGLPILTE GKEKAPRPAP APQAPAQNTT
     PVTKTRLIDT PVRSGQRIYA PQCDLIVTSH VSAGAELIAD GNIHVYGMMR GRALAGASGD
     RETQIFCTNL MAELVSIAGE YWLSDQIPAE FYGKAARLQL VENALTVQPL N
 
 
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