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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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