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Protein

Septum site-determining protein MinD

Gene

minD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: EcoCyc
  • ATP binding Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • barrier septum site selection Source: InterPro
  • cell division Source: EcoCyc
  • chromosome segregation Source: EcoCyc
  • negative regulation of cell division Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10597-MONOMER.
ECOL316407:JW1164-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Septum site-determining protein MinD
Alternative name(s):
Cell division inhibitor MinD
Gene namesi
Name:minD
Ordered Locus Names:b1175, JW1164
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10597. minD.

Subcellular locationi

GO - Cellular componenti

  • cell pole Source: EcoCyc
  • cytoplasmic side of plasma membrane Source: EcoCyc
  • cytosol Source: EcoCyc
  • intrinsic component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

In a minCDE operon disruption (minC-minD-minE), cells divide not only at midpoint but also at their poles, yielding small minicells and long rods. Loss of polar localization of several polar-localized proteins including GroEL-GroES, TnaA and YqjD.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151G → S: Less effective then wild-type. 1 Publication
Mutagenesisi16 – 172KT → QR: Loss of activity. 1 Publication
Mutagenesisi16 – 161K → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 270269Septum site-determining protein MinDPRO_0000201968Add
BLAST

Proteomic databases

EPDiP0AEZ3.
PaxDbiP0AEZ3.
PRIDEiP0AEZ3.

2D gel databases

SWISS-2DPAGEP0AEZ3.

Interactioni

Subunit structurei

Interacts with MinC and FtsZ.

Binary interactionsi

WithEntry#Exp.IntActNotes
minCP181966EBI-554545,EBI-554060
minEP0A7344EBI-554545,EBI-1118020

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262868. 668 interactions.
DIPiDIP-35946N.
IntActiP0AEZ3. 13 interactions.
STRINGi511145.b1175.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi10 – 156Combined sources
Helixi16 – 2914Combined sources
Beta strandi34 – 385Combined sources
Helixi46 – 494Combined sources
Helixi53 – 553Combined sources
Helixi60 – 645Combined sources
Helixi70 – 734Combined sources
Beta strandi78 – 803Combined sources
Beta strandi83 – 864Combined sources
Helixi99 – 11113Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi123 – 1264Combined sources
Helixi127 – 1348Combined sources
Beta strandi137 – 1437Combined sources
Helixi147 – 16014Combined sources
Helixi165 – 1684Combined sources
Beta strandi175 – 1839Combined sources
Helixi185 – 1895Combined sources
Helixi196 – 2038Combined sources
Beta strandi205 – 2128Combined sources
Helixi216 – 2238Combined sources
Helixi227 – 2293Combined sources
Helixi234 – 24613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q9LX-ray2.34A/B1-260[»]
3R9IX-ray2.60A/B/C/D1-260[»]
3R9JX-ray4.30A/B1-260[»]
ProteinModelPortaliP0AEZ3.
SMRiP0AEZ3. Positions 2-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ParA family. MinD subfamily.Curated

Phylogenomic databases

eggNOGiENOG4107QMS. Bacteria.
COG2894. LUCA.
HOGENOMiHOG000019419.
InParanoidiP0AEZ3.
KOiK03609.
OMAiVNRIRNH.
OrthoDBiEOG6NPMB6.
PhylomeDBiP0AEZ3.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002586. CobQ/CobB/MinD/ParA_Nub-bd_dom.
IPR025501. MinD.
IPR010223. MinD_bac-type.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01656. CbiA. 1 hit.
[Graphical view]
PIRSFiPIRSF003092. MinD. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01968. minD_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARIIVVTSG KGGVGKTTSS AAIATGLAQK GKKTVVIDFD IGLRNLDLIM
60 70 80 90 100
GCERRVVYDF VNVIQGDATL NQALIKDKRT ENLYILPASQ TRDKDALTRE
110 120 130 140 150
GVAKVLDDLK AMDFEFIVCD SPAGIETGAL MALYFADEAI ITTNPEVSSV
160 170 180 190 200
RDSDRILGIL ASKSRRAENG EEPIKEHLLL TRYNPGRVSR GDMLSMEDVL
210 220 230 240 250
EILRIKLVGV IPEDQSVLRA SNQGEPVILD INADAGKAYA DTVERLLGEE
260 270
RPFRFIEEEK KGFLKRLFGG
Length:270
Mass (Da):29,614
Last modified:January 23, 2007 - v2
Checksum:i0D2C4C0976B77D2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03153 Genomic DNA. Translation: AAB59062.1.
U00096 Genomic DNA. Translation: AAC74259.1.
AP009048 Genomic DNA. Translation: BAA36009.1.
PIRiB31877. CCECID.
RefSeqiNP_415693.1. NC_000913.3.
WP_000101055.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74259; AAC74259; b1175.
BAA36009; BAA36009; BAA36009.
GeneIDi945741.
KEGGiecj:JW1164.
eco:b1175.
PATRICi32117594. VBIEscCol129921_1219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03153 Genomic DNA. Translation: AAB59062.1.
U00096 Genomic DNA. Translation: AAC74259.1.
AP009048 Genomic DNA. Translation: BAA36009.1.
PIRiB31877. CCECID.
RefSeqiNP_415693.1. NC_000913.3.
WP_000101055.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q9LX-ray2.34A/B1-260[»]
3R9IX-ray2.60A/B/C/D1-260[»]
3R9JX-ray4.30A/B1-260[»]
ProteinModelPortaliP0AEZ3.
SMRiP0AEZ3. Positions 2-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262868. 668 interactions.
DIPiDIP-35946N.
IntActiP0AEZ3. 13 interactions.
STRINGi511145.b1175.

2D gel databases

SWISS-2DPAGEP0AEZ3.

Proteomic databases

EPDiP0AEZ3.
PaxDbiP0AEZ3.
PRIDEiP0AEZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74259; AAC74259; b1175.
BAA36009; BAA36009; BAA36009.
GeneIDi945741.
KEGGiecj:JW1164.
eco:b1175.
PATRICi32117594. VBIEscCol129921_1219.

Organism-specific databases

EchoBASEiEB0592.
EcoGeneiEG10597. minD.

Phylogenomic databases

eggNOGiENOG4107QMS. Bacteria.
COG2894. LUCA.
HOGENOMiHOG000019419.
InParanoidiP0AEZ3.
KOiK03609.
OMAiVNRIRNH.
OrthoDBiEOG6NPMB6.
PhylomeDBiP0AEZ3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10597-MONOMER.
ECOL316407:JW1164-MONOMER.

Miscellaneous databases

PROiP0AEZ3.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002586. CobQ/CobB/MinD/ParA_Nub-bd_dom.
IPR025501. MinD.
IPR010223. MinD_bac-type.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01656. CbiA. 1 hit.
[Graphical view]
PIRSFiPIRSF003092. MinD. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01968. minD_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli."
    de Boer P.A.J., Crossley R.E., Rothfield L.I.
    Cell 56:641-649(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  6. "The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site."
    de Boer P.A.J., Crossley R.E., Hand A.R., Rothfield L.I.
    EMBO J. 10:4371-4380(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS.
  7. "Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli."
    Raskin D.M., de Boer P.A.J.
    Proc. Natl. Acad. Sci. U.S.A. 96:4971-4976(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli."
    Li G., Young K.D.
    Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUBCELLULAR LOCATION AT CELL POLES, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiMIND_ECOLI
AccessioniPrimary (citable) accession number: P0AEZ3
Secondary accession number(s): P18197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.