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Protein

Cell shape-determining protein MreC

Gene

mreC

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

Functioni

Involved in formation and maintenance of cell shape. Responsible for formation of rod shape. May also contribute to regulation of formation of penicillin-binding proteins.2 Publications

GO - Molecular functioni

  • protein self-association Source: UniProtKB

GO - Biological processi

  • establishment or maintenance of cell polarity regulating cell shape Source: UniProtKB
  • regulation of cell shape Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

BioCyciEcoCyc:EG10609-MONOMER.
ECOL316407:JW3219-MONOMER.

Protein family/group databases

TCDBi9.B.157.1.3. the cell shape-determining mrebcd (mrebcd) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell shape-determining protein MreC
Alternative name(s):
Cell shape protein MreC
Rod shape-determining protein MreC
Gene namesi
Name:mreC
Ordered Locus Names:b3250, JW3219
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10609. mreC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3523HelicalSequence analysisAdd
BLAST
Topological domaini36 – 367332PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Reduction in growth rate and ultimately cell lysis. Growth arrest is associated with remarkable change in cell morphology from the normal rod-shape to enlarged, spherical cells. Many of the large spherical cells lyse at a later stage.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Cell shape-determining protein MreCPRO_0000062767Add
BLAST

Proteomic databases

PaxDbiP16926.
PRIDEiP16926.

Interactioni

Subunit structurei

Self-associates. Interacts with MreB and MreD.1 Publication

GO - Molecular functioni

  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi4261941. 220 interactions.
DIPiDIP-10256N.
IntActiP16926. 5 interactions.
MINTiMINT-7012243.
STRINGi511145.b3250.

Structurei

3D structure databases

ProteinModelPortaliP16926.
SMRiP16926. Positions 76-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili63 – 9230Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi279 – 36789Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the MreC family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105N3I. Bacteria.
COG1792. LUCA.
HOGENOMiHOG000266097.
InParanoidiP16926.
KOiK03570.
OMAiVELMPYT.
PhylomeDBiP16926.

Family and domain databases

InterProiIPR007221. MreC.
[Graphical view]
PfamiPF04085. MreC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00219. mreC. 1 hit.

Sequencei

Sequence statusi: Complete.

P16926-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPIFSRGPS LQIRLILAVL VALGIIIADS RLGTFSQIRT YMDTAVSPFY
60 70 80 90 100
FVSNAPRELL DGVSQTLASR DQLELENRAL RQELLLKNSE LLMLGQYKQE
110 120 130 140 150
NARLRELLGS PLRQDEQKMV TQVISTVNDP YSDQVVIDKG SVNGVYEGQP
160 170 180 190 200
VISDKGVVGQ VVAVAKLTSR VLLICDATHA LPIQVLRNDI RVIAAGNGCT
210 220 230 240 250
DDLQLEHLPA NTDIRVGDVL VTSGLGGRFP EGYPVAVVSS VKLDTQRAYT
260 270 280 290 300
VIQARPTAGL QRLRYLLLLW GADRNGANPM TPEEVHRVAN ERLMQMMPQV
310 320 330 340 350
LPSPDAMGPK LPEPATGIAQ PTPQQPATGN AATAPAAPTQ PAANRSPQRA
360
TPPQSGAQPP ARAPGGQ
Length:367
Mass (Da):39,530
Last modified:August 1, 1990 - v1
Checksum:i1BAA7C5EF9E84C92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31792 Genomic DNA. Translation: AAA24155.1.
U18997 Genomic DNA. Translation: AAA58053.1.
U00096 Genomic DNA. Translation: AAC76282.1.
AP009048 Genomic DNA. Translation: BAE77292.1.
M22055 Genomic DNA. Translation: AAA83892.1.
PIRiJV0059.
RefSeqiNP_417716.1. NC_000913.3.
WP_000802511.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76282; AAC76282; b3250.
BAE77292; BAE77292; BAE77292.
GeneIDi947655.
KEGGiecj:JW3219.
eco:b3250.
PATRICi32121926. VBIEscCol129921_3347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31792 Genomic DNA. Translation: AAA24155.1.
U18997 Genomic DNA. Translation: AAA58053.1.
U00096 Genomic DNA. Translation: AAC76282.1.
AP009048 Genomic DNA. Translation: BAE77292.1.
M22055 Genomic DNA. Translation: AAA83892.1.
PIRiJV0059.
RefSeqiNP_417716.1. NC_000913.3.
WP_000802511.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP16926.
SMRiP16926. Positions 76-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261941. 220 interactions.
DIPiDIP-10256N.
IntActiP16926. 5 interactions.
MINTiMINT-7012243.
STRINGi511145.b3250.

Protein family/group databases

TCDBi9.B.157.1.3. the cell shape-determining mrebcd (mrebcd) family.

Proteomic databases

PaxDbiP16926.
PRIDEiP16926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76282; AAC76282; b3250.
BAE77292; BAE77292; BAE77292.
GeneIDi947655.
KEGGiecj:JW3219.
eco:b3250.
PATRICi32121926. VBIEscCol129921_3347.

Organism-specific databases

EchoBASEiEB0604.
EcoGeneiEG10609. mreC.

Phylogenomic databases

eggNOGiENOG4105N3I. Bacteria.
COG1792. LUCA.
HOGENOMiHOG000266097.
InParanoidiP16926.
KOiK03570.
OMAiVELMPYT.
PhylomeDBiP16926.

Enzyme and pathway databases

BioCyciEcoCyc:EG10609-MONOMER.
ECOL316407:JW3219-MONOMER.

Miscellaneous databases

PROiP16926.

Family and domain databases

InterProiIPR007221. MreC.
[Graphical view]
PfamiPF04085. MreC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00219. mreC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMREC_ECOLI
AccessioniPrimary (citable) accession number: P16926
Secondary accession number(s): P13028, Q2M8W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 7, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.