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Protein

Cell shape-determining protein MreB

Gene

mreB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:15612918, PubMed:21903929). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:21903929). A feedback loop between cell geometry and MreB localization maintains elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (PubMed:24550515). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization (PubMed:21903929). Rotation may contribute to the robust maintenance of rod shape (PubMed:21903929).3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Requires ATP hydrolysis for polymerization (PubMed:23235161). Polymerization is inhibited by toxins CbtA and CptA, as well as by A22 ([S-(3,4-dichlorobenzyl)isothiourea)] all of which cause cell rounding and eventual death. Inhibition by toxin CbtA is neutralized by cytoskeleton bundling-enhancing protein CbeA, inhibition by toxin CptA is neutralized by antitoxin CptB, while inhibition by A22 can be neutralized by overexpression of CbeA (PubMed:21166897, PubMed:22239607, PubMed:22515815).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi19 – 21ATPUniRule annotation3
Nucleotide bindingi168 – 170ATPUniRule annotation3
Nucleotide bindingi216 – 219ATPUniRule annotation4
Nucleotide bindingi296 – 299ATPUniRule annotation4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • identical protein binding Source: EcoCyc

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell shape
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10608-MONOMER

Protein family/group databases

Transport Classification Database

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cell shape-determining protein MreBUniRule annotationCurated
Alternative name(s):
Actin-like MreB proteinCurated
Rod shape-determining protein MreBCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mreB1 Publication
Synonyms:envB, rodY
Ordered Locus Names:b3251, JW3220
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10608 mreB

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Depletion results in enlarged, spherical cells.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000627591 – 347Cell shape-determining protein MreBAdd BLAST347

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A9X4

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A9X4

PRoteomics IDEntifications database

More...
PRIDEi
P0A9X4

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms polymers in the presence of ATP or GTP (PubMed:23235161). Forms an essential membrane-bound complex with MreC and MreD. Interacts directly with MreC but not with MreD (PubMed:15612918). Interacts with FtsZ, toxins CbtA and CptA, and cytoskeleton bundling-enhancing protein CbeA (PubMed:21166897, PubMed:22239607, PubMed:22515815).5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261940, 383 interactors

Database of interacting proteins

More...
DIPi
DIP-31874N

Protein interaction database and analysis system

More...
IntActi
P0A9X4, 81 interactors

Molecular INTeraction database

More...
MINTi
P0A9X4

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3427

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A9X4

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A9X4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the FtsA/MreB family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1077 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000019757

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9X4

KEGG Orthology (KO)

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KOi
K03569

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9X4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10225 MreB_like, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02207 MreB, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004753 MreB

The PANTHER Classification System

More...
PANTHERi
PTHR42749 PTHR42749, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06723 MreB_Mbl, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01652 SHAPEPROTEIN

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00904 mreB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A9X4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLKKFRGMFS NDLSIDLGTA NTLIYVKGQG IVLNEPSVVA IRQDRAGSPK
60 70 80 90 100
SVAAVGHDAK QMLGRTPGNI AAIRPMKDGV IADFFVTEKM LQHFIKQVHS
110 120 130 140 150
NSFMRPSPRV LVCVPVGATQ VERRAIRESA QGAGAREVFL IEEPMAAAIG
160 170 180 190 200
AGLPVSEATG SMVVDIGGGT TEVAVISLNG VVYSSSVRIG GDRFDEAIIN
210 220 230 240 250
YVRRNYGSLI GEATAERIKH EIGSAYPGDE VREIEVRGRN LAEGVPRGFT
260 270 280 290 300
LNSNEILEAL QEPLTGIVSA VMVALEQCPP ELASDISERG MVLTGGGALL
310 320 330 340
RNLDRLLMEE TGIPVVVAED PLTCVARGGG KALEMIDMHG GDLFSEE
Length:347
Mass (Da):36,952
Last modified:September 13, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1393696D8CDAEF93
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA58054 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti60 – 61KQ → NE in AAA83891 (PubMed:3049542).Curated2
Sequence conflicti265T → I in AAA83891 (PubMed:3049542).Curated1
Sequence conflicti277 – 278QC → HT in AAA83891 (PubMed:3049542).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M22055 Genomic DNA Translation: AAA83891.1
U18997 Genomic DNA Translation: AAA58054.1 Different initiation.
U00096 Genomic DNA Translation: AAC76283.2
AP009048 Genomic DNA Translation: BAE77293.1
M31792 Genomic DNA Translation: AAA24154.1

NCBI Reference Sequences

More...
RefSeqi
NP_417717.2, NC_000913.3
WP_000913396.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76283; AAC76283; b3251
BAE77293; BAE77293; BAE77293

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
34152801
948588

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3220
eco:b3251

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3348

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22055 Genomic DNA Translation: AAA83891.1
U18997 Genomic DNA Translation: AAA58054.1 Different initiation.
U00096 Genomic DNA Translation: AAC76283.2
AP009048 Genomic DNA Translation: BAE77293.1
M31792 Genomic DNA Translation: AAA24154.1
RefSeqiNP_417717.2, NC_000913.3
WP_000913396.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP0A9X4
SMRiP0A9X4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261940, 383 interactors
DIPiDIP-31874N
IntActiP0A9X4, 81 interactors
MINTiP0A9X4
STRINGi316385.ECDH10B_3427

Protein family/group databases

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

Proteomic databases

EPDiP0A9X4
PaxDbiP0A9X4
PRIDEiP0A9X4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76283; AAC76283; b3251
BAE77293; BAE77293; BAE77293
GeneIDi34152801
948588
KEGGiecj:JW3220
eco:b3251
PATRICifig|511145.12.peg.3348

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0603
EcoGeneiEG10608 mreB

Phylogenomic databases

eggNOGiCOG1077 LUCA
HOGENOMiHOG000019757
InParanoidiP0A9X4
KOiK03569
PhylomeDBiP0A9X4

Enzyme and pathway databases

BioCyciEcoCyc:EG10608-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0A9X4

Family and domain databases

CDDicd10225 MreB_like, 1 hit
HAMAPiMF_02207 MreB, 1 hit
InterProiView protein in InterPro
IPR004753 MreB
PANTHERiPTHR42749 PTHR42749, 1 hit
PfamiView protein in Pfam
PF06723 MreB_Mbl, 1 hit
PRINTSiPR01652 SHAPEPROTEIN
TIGRFAMsiTIGR00904 mreB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMREB_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A9X4
Secondary accession number(s): P13519, P76678, Q2M8W3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: December 5, 2018
This is version 102 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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