MINC_ECOLC
ID MINC_ECOLC Reviewed; 231 AA.
AC B1IUB5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=EcolC_2449;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-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}.
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; CP000946; ACA78082.1; -; Genomic_DNA.
DR RefSeq; WP_001301105.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IUB5; -.
DR SMR; B1IUB5; -.
DR KEGG; ecl:EcolC_2449; -.
DR HOGENOM; CLU_067812_0_1_6; -.
DR OMA; RRDPLWG; -.
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="Probable septum site-determining protein MinC"
FT /id="PRO_1000078653"
FT REGION 101..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 24776 MW; E4283A6AD850DAD0 CRC64;
MSNTPIELKG SSFTLSVVHL HEAEPKVIHQ ALEDKIAQAP AFLKHAPVVL NVSALEDPVN
WSAMHKAVSA TGLRVIGVSG CKDAQLKAEI EKMGLPILTE GKEKAPRPAP TPQAPAQNTT
PVTKTRLIDT PVRSGQRIYA PQCDLIVTSH VSAGAELIAD GNIHVYGMMR GRALAGASGD
RETQIFCTNL MAELVSIAGE YWLSDQIPAE FYGKAARLQL VENALTVQPL N