MINC_ECOLI
ID MINC_ECOLI Reviewed; 231 AA.
AC P18196;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Septum site-determining protein MinC;
GN Name=minC; OrderedLocusNames=b1176, JW1165;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2645057; DOI=10.1016/0092-8674(89)90586-2;
RA de Boer P.A.J., Crossley R.E., Rothfield L.I.;
RT "A division inhibitor and a topological specificity factor coded for by the
RT minicell locus determine proper placement of the division septum in E.
RT coli.";
RL Cell 56:641-649(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10611296; DOI=10.1073/pnas.96.26.14819;
RA Hu Z., Mukherjee A., Pichoff S., Lutkenhaus J.;
RT "The MinC component of the division site selection system in Escherichia
RT coli interacts with FtsZ to prevent polymerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14819-14824(1999).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10869074; DOI=10.1128/jb.182.14.3965-3971.2000;
RA Hu Z., Lutkenhaus J.;
RT "Analysis of MinC reveals two independent domains involved in interaction
RT with MinD and FtsZ.";
RL J. Bacteriol. 182:3965-3971(2000).
RN [7]
RP FUNCTION IN LOCATION AT CELL POLES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
RA Li G., Young K.D.;
RT "Isolation and identification of new inner membrane-associated proteins
RT that localize to cell poles in Escherichia coli.";
RL Mol. Microbiol. 84:276-295(2012).
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.
CC {ECO:0000269|PubMed:22380631}.
CC -!- SUBUNIT: Interacts with MinD and FtsZ; homodimer.
CC -!- INTERACTION:
CC P18196; P0AEJ8: eutN; NbExp=3; IntAct=EBI-554060, EBI-8767793;
CC P18196; P00946: manA; NbExp=5; IntAct=EBI-554060, EBI-554045;
CC P18196; P0AEZ3: minD; NbExp=7; IntAct=EBI-554060, EBI-554545;
CC P18196; P39409: yjjW; NbExp=2; IntAct=EBI-554060, EBI-9132384;
CC -!- DISRUPTION PHENOTYPE: In a minCDE operon disruption (minC-minD-minE),
CC cells divide not only at midpoint but also at their poles, yielding
CC small minicells and long rods. Loss of polar localization of several
CC polar-localized proteins including GroEL-GroES, TnaA and YqjD.
CC {ECO:0000269|PubMed:22380631}.
CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000305}.
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DR EMBL; J03153; AAB59061.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74260.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36010.1; -; Genomic_DNA.
DR PIR; A31877; CEECIC.
DR RefSeq; NP_415694.1; NC_000913.3.
DR RefSeq; WP_001301105.1; NZ_SSZK01000010.1.
DR AlphaFoldDB; P18196; -.
DR SMR; P18196; -.
DR BioGRID; 4260098; 287.
DR BioGRID; 850111; 22.
DR DIP; DIP-10214N; -.
DR IntAct; P18196; 32.
DR MINT; P18196; -.
DR STRING; 511145.b1176; -.
DR jPOST; P18196; -.
DR PaxDb; P18196; -.
DR PRIDE; P18196; -.
DR DNASU; 945744; -.
DR EnsemblBacteria; AAC74260; AAC74260; b1176.
DR EnsemblBacteria; BAA36010; BAA36010; BAA36010.
DR GeneID; 945744; -.
DR KEGG; ecj:JW1165; -.
DR KEGG; eco:b1176; -.
DR PATRIC; fig|1411691.4.peg.1112; -.
DR EchoBASE; EB0591; -.
DR eggNOG; COG0850; Bacteria.
DR HOGENOM; CLU_067812_0_1_6; -.
DR InParanoid; P18196; -.
DR OMA; RRDPLWG; -.
DR PhylomeDB; P18196; -.
DR BioCyc; EcoCyc:EG10596-MON; -.
DR PRO; PR:P18196; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; EXP:EcoliWiki.
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; EXP:EcoliWiki.
DR GO; GO:0032955; P:regulation of division septum assembly; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Reference proteome; Septation.
FT CHAIN 1..231
FT /note="Septum site-determining protein MinC"
FT /id="PRO_0000189033"
FT REGION 101..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 10
FT /note="G -> D (in minC19; reduces affinity of MinC for
FT FtsZ)"
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