MIND_ECOLI
ID MIND_ECOLI Reviewed; 270 AA.
AC P0AEZ3; P18197;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Septum site-determining protein MinD;
DE AltName: Full=Cell division inhibitor MinD;
GN Name=minD; OrderedLocusNames=b1175, JW1164;
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 PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=1836760;
RA de Boer P.A.J., Crossley R.E., Hand A.R., Rothfield L.I.;
RT "The MinD protein is a membrane ATPase required for the correct placement
RT of the Escherichia coli division site.";
RL EMBO J. 10:4371-4380(1991).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10220403; DOI=10.1073/pnas.96.9.4971;
RA Raskin D.M., de Boer P.A.J.;
RT "Rapid pole-to-pole oscillation of a protein required for directing
RT division to the middle of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4971-4976(1999).
RN [8]
RP FUNCTION IN SUBCELLULAR 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: ATPase required for the correct placement of the division
CC site. Cell division inhibitors MinC and MinD act in concert to form an
CC inhibitor capable of blocking formation of the polar Z ring septums.
CC Rapidly oscillates between the poles of the cell to destabilize FtsZ
CC filaments that have formed before they mature into polar Z rings.
CC {ECO:0000269|PubMed:1836760, ECO:0000269|PubMed:22380631}.
CC -!- SUBUNIT: Interacts with MinC and FtsZ.
CC -!- INTERACTION:
CC P0AEZ3; P18196: minC; NbExp=7; IntAct=EBI-554545, EBI-554060;
CC P0AEZ3; P0A734: minE; NbExp=4; IntAct=EBI-554545, EBI-1118020;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
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 ParA family. MinD subfamily. {ECO:0000305}.
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DR EMBL; J03153; AAB59062.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74259.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36009.1; -; Genomic_DNA.
DR PIR; B31877; CCECID.
DR RefSeq; NP_415693.1; NC_000913.3.
DR RefSeq; WP_000101055.1; NZ_STEB01000023.1.
DR PDB; 3Q9L; X-ray; 2.34 A; A/B=1-260.
DR PDB; 3R9I; X-ray; 2.60 A; A/B/C/D=1-260.
DR PDB; 3R9J; X-ray; 4.30 A; A/B=1-260.
DR PDBsum; 3Q9L; -.
DR PDBsum; 3R9I; -.
DR PDBsum; 3R9J; -.
DR AlphaFoldDB; P0AEZ3; -.
DR SMR; P0AEZ3; -.
DR BioGRID; 4262868; 690.
DR BioGRID; 850108; 3.
DR DIP; DIP-35946N; -.
DR IntAct; P0AEZ3; 15.
DR MINT; P0AEZ3; -.
DR STRING; 511145.b1175; -.
DR SWISS-2DPAGE; P0AEZ3; -.
DR jPOST; P0AEZ3; -.
DR PaxDb; P0AEZ3; -.
DR PRIDE; P0AEZ3; -.
DR EnsemblBacteria; AAC74259; AAC74259; b1175.
DR EnsemblBacteria; BAA36009; BAA36009; BAA36009.
DR GeneID; 66675005; -.
DR GeneID; 945741; -.
DR KEGG; ecj:JW1164; -.
DR KEGG; eco:b1175; -.
DR PATRIC; fig|1411691.4.peg.1113; -.
DR EchoBASE; EB0592; -.
DR eggNOG; COG2894; Bacteria.
DR HOGENOM; CLU_037612_0_1_6; -.
DR InParanoid; P0AEZ3; -.
DR OMA; CESAKAY; -.
DR PhylomeDB; P0AEZ3; -.
DR BioCyc; EcoCyc:EG10597-MON; -.
DR PRO; PR:P0AEZ3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IDA:EcoCyc.
DR GO; GO:0007059; P:chromosome segregation; IMP:EcoCyc.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051782; P:negative regulation of cell division; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13614; AAA_31; 1.
DR PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01968; minD_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Direct protein sequencing; Membrane; Nucleotide-binding;
KW Reference proteome; Septation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..270
FT /note="Septum site-determining protein MinD"
FT /id="PRO_0000201968"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q72H90"
FT MUTAGEN 15
FT /note="G->S: Less effective then wild-type."
FT /evidence="ECO:0000269|PubMed:1836760"
FT MUTAGEN 16..17
FT /note="KT->QR: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1836760"
FT MUTAGEN 16
FT /note="K->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1836760"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:3R9I"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:3Q9L"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3Q9L"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3Q9L"
SQ SEQUENCE 270 AA; 29614 MW; 0D2C4C0976B77D2C CRC64;
MARIIVVTSG KGGVGKTTSS AAIATGLAQK GKKTVVIDFD IGLRNLDLIM GCERRVVYDF
VNVIQGDATL NQALIKDKRT ENLYILPASQ TRDKDALTRE GVAKVLDDLK AMDFEFIVCD
SPAGIETGAL MALYFADEAI ITTNPEVSSV RDSDRILGIL ASKSRRAENG EEPIKEHLLL
TRYNPGRVSR GDMLSMEDVL EILRIKLVGV IPEDQSVLRA SNQGEPVILD INADAGKAYA
DTVERLLGEE RPFRFIEEEK KGFLKRLFGG
