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UniProtKB - P39751 (MBL_BACSU)

Entry version 123 (02 Dec 2020)
Sequence version 1 (01 Feb 1995)
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Protein

Cell shape-determining protein Mbl

Gene

mbl

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score:

Annotation score:4 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:11290328, PubMed:19659933). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:19659933). A feedback loop between cell geometry and Mbl localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). 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 Mbl polymerization (PubMed:21636745, PubMed:21636744). Organizes peptidoglycan synthesis in the lateral cell wall (PubMed:19659933). Also required for proper chromosome segregation (PubMed:14588250).By similarity5 Publications

Miscellaneous

B.subtilis has three MreB paralogs: MreB, Mbl and MreBH. All paralogs have the ability to support rod-shaped cell growth normal conditions. The multiplicity of paralogs becomes important under stress conditions. They are probably used to allow cells to maintain proper growth and morphogenesis under changing conditions.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi12 – 14ATPUniRule annotation3
Nucleotide bindingi156 – 158ATPUniRule annotation3
Nucleotide bindingi204 – 207ATPUniRule annotation4
Nucleotide bindingi284 – 287ATPUniRule 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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		BSUB:BSU36410-MONOMER

<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%5Fand%5Ftaxonomy%5Fsection">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 MblCurated
Alternative name(s):
Actin-like Mbl proteinCurated
Rod shape-determining protein MblCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:mbl
Ordered Locus Names:BSU36410
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

Complete GO annotation on QuickGO ...

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

Mutants are bent and twisted at irregular angles (PubMed:11290328). Depletion leads to a strong defect in chromosome segregation (PubMed:14588250).2 Publications

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000627551 – 333Cell shape-determining protein MblAdd BLAST333

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P39751

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

More...PaxDbi		P39751

PRoteomics IDEntifications database

More...PRIDEi		P39751

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms polymers (PubMed:11290328, PubMed:19659933).

Forms a complex with MreB and MreBH (PubMed:17064365, PubMed:19659933).

Interacts with MreC (PubMed:17064365).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-52430N

Protein interaction database and analysis system

More...IntActi		P39751, 2 interactors

STRING: functional protein association networks

More...STRINGi		224308.BSU36410

<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

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

More...SMRi		P39751

Database of comparative protein structure models

More...ModBasei		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, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P39751

Identification of Orthologs from Complete Genome Data

More...OMAi		MDIFQPS

Database for complete collections of gene phylogenies

More...PhylomeDBi		P39751

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
IPR043129, ATPase_NBD
IPR004753, MreB

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01652, SHAPEPROTEIN

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53067, SSF53067, 2 hits

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P39751-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFARDIGIDL GTANVLIHVK GKGIVLNEPS VVALDKNSGK VLAVGEEARR 
        60         70         80         90        100
MVGRTPGNIV AIRPLKDGVI ADFEVTEAML KHFINKLNVK GLFSKPRMLI 
       110        120        130        140        150
CCPTNITSVE QKAIKEAAEK SGGKHVYLEE EPKVAAIGAG MEIFQPSGNM 
       160        170        180        190        200
VVDIGGGTTD IAVISMGDIV TSSSIKMAGD KFDMEILNYI KREYKLLIGE 
       210        220        230        240        250
RTAEDIKIKV ATVFPDARHE EISIRGRDMV SGLPRTITVN SKEVEEALRE 
       260        270        280        290        300
SVAVIVQAAK QVLERTPPEL SADIIDRGVI ITGGGALLNG LDQLLAEELK 
       310        320        330 
VPVLVAENPM DCVAIGTGVM LDNMDKLPKR KLS
Length:333
Mass (Da):35,861
Last modified:February 1, 1995 - 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:iD1599B7EEDEAF8A9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U12962 Genomic DNA Translation: AAA67878.1
AL009126 Genomic DNA Translation: CAB15658.2
Z82987 Genomic DNA Translation: CAB05381.1

Protein sequence database of the Protein Information Resource

More...PIRi		I40531

NCBI Reference Sequences

More...RefSeqi		NP_391522.2, NC_000964.3
WP_003227776.1, NZ_JNCM01000034.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CAB15658; CAB15658; BSU36410

Database of genes from NCBI RefSeq genomes

More...GeneIDi		51992854
936916

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bsu:BSU36410

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224308.179.peg.3941

<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
U12962 Genomic DNA Translation: AAA67878.1
AL009126 Genomic DNA Translation: CAB15658.2
Z82987 Genomic DNA Translation: CAB05381.1
PIRiI40531
RefSeqiNP_391522.2, NC_000964.3
WP_003227776.1, NZ_JNCM01000034.1

3D structure databases

SMRiP39751
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-52430N
IntActiP39751, 2 interactors
STRINGi224308.BSU36410

Proteomic databases

jPOSTiP39751
PaxDbiP39751
PRIDEiP39751

Genome annotation databases

EnsemblBacteriaiCAB15658; CAB15658; BSU36410
GeneIDi51992854
936916
KEGGibsu:BSU36410
PATRICifig|224308.179.peg.3941

Phylogenomic databases

eggNOGiCOG1077, Bacteria
InParanoidiP39751
OMAiMDIFQPS
PhylomeDBiP39751

Enzyme and pathway databases

BioCyciBSUB:BSU36410-MONOMER

Family and domain databases

CDDicd10225, MreB_like, 1 hit
HAMAPiMF_02207, MreB, 1 hit
InterProiView protein in InterPro
IPR043129, ATPase_NBD
IPR004753, MreB
PRINTSiPR01652, SHAPEPROTEIN
SUPFAMiSSF53067, SSF53067, 2 hits
TIGRFAMsiTIGR00904, mreB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiMBL_BACSU
<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: P39751
Secondary accession number(s): O32275
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 2, 2020
This is version 123 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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