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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 18ATPBy similarity8

GO - Molecular functioni

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

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi15G → S: Less effective then wild-type. 1 Publication1
Mutagenesisi16 – 17KT → QR: Loss of activity. 1 Publication2
Mutagenesisi16K → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002019682 – 270Septum site-determining protein MinDAdd BLAST269

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 interactors.
DIPiDIP-35946N.
IntActiP0AEZ3. 13 interactors.
STRINGi511145.b1175.

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Beta strandi10 – 15Combined sources6
Helixi16 – 29Combined sources14
Beta strandi34 – 38Combined sources5
Helixi46 – 49Combined sources4
Helixi53 – 55Combined sources3
Helixi60 – 64Combined sources5
Helixi70 – 73Combined sources4
Beta strandi78 – 80Combined sources3
Beta strandi83 – 86Combined sources4
Helixi99 – 111Combined sources13
Beta strandi115 – 120Combined sources6
Beta strandi123 – 126Combined sources4
Helixi127 – 134Combined sources8
Beta strandi137 – 143Combined sources7
Helixi147 – 160Combined sources14
Helixi165 – 168Combined sources4
Beta strandi175 – 183Combined sources9
Helixi185 – 189Combined sources5
Helixi196 – 203Combined sources8
Beta strandi205 – 212Combined sources8
Helixi216 – 223Combined sources8
Helixi227 – 229Combined sources3
Helixi234 – 246Combined sources13

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the ParA family. MinD subfamily.Curated

Phylogenomic databases

eggNOGiENOG4107QMS. Bacteria.
COG2894. LUCA.
HOGENOMiHOG000019419.
InParanoidiP0AEZ3.
KOiK03609.
OMAiNRVRPKM.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3Q9LX-ray2.34A/B1-260[»]
3R9IX-ray2.60A/B/C/D1-260[»]
3R9JX-ray4.30A/B1-260[»]
ProteinModelPortaliP0AEZ3.
SMRiP0AEZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262868. 668 interactors.
DIPiDIP-35946N.
IntActiP0AEZ3. 13 interactors.
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.
OMAiNRVRPKM.
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...

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: November 30, 2016
This is version 100 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.