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UniProtKB - P29131 (FTSN_ECOLI)

Entry version 176 (07 Apr 2021)
Sequence version 3 (29 Aug 2003)
Previous versions | rss
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Protein

Cell division protein FtsN

Gene

ftsN

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

Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases (Probable) (PubMed:25496160). Required for full FtsI activity (PubMed:25496160). Required for recruitment of AmiC to the septal ring (PubMed:12787347).2 Publications2 Publications

<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

  • cell division Source: CACAO
  • division septum assembly Source: EcoCyc
  • FtsZ-dependent cytokinesis Source: UniProtKB-UniRule
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 cycle, Cell division, Septation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11529-MONOMER
MetaCyc:EG11529-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 division protein FtsNUniRule annotationCurated
<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:ftsNUniRule annotation
Synonyms:msgA
Ordered Locus Names:b3933, JW3904
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <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
  • UP000000625 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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 33CytoplasmicUniRule annotation1 PublicationAdd BLAST33
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei34 – 54HelicalUniRule annotationAdd BLAST21
Topological domaini55 – 319PeriplasmicUniRule annotation1 PublicationAdd BLAST265

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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 does not affect localization of FtsZ, FtsA, ZipA, FtsQ, FtsL and FtsI to the division site (PubMed:11703663). Cells containing low levels of FtsN stop dividing while their mean cell length increases (PubMed:20345660). Absence of FtsN is followed by an inverse sequential disassembly of already assembled divisome compounds (PubMed:20345660).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi5D → N: Causes significant impairment of the interaction with FtsA. 1 Publication1
Mutagenesisi83W → L or T: Lack of activity. 1 Publication1
Mutagenesisi85Y → S or W: Lack of activity. 1 Publication1
Mutagenesisi89L → S: Lack of activity. 1 Publication1
Mutagenesisi251Q → A: Reduces septal localization by a factor of at least 3. 1 Publication1
Mutagenesisi251Q → E: Severe localization defects. Binds peptidoglycan poorly. 1 Publication1
Mutagenesisi252C → A: Severely reduces stability of the protein. 1 Publication1
Mutagenesisi254S → A: Reduces septal localization by a factor of at least 3. 1 Publication1
Mutagenesisi254S → E: Binds peptidoglycan poorly. 1 Publication1
Mutagenesisi263T → D: Intermediate localization defects. 1 Publication1
Mutagenesisi270F → A: Intermediate localization defects. 1 Publication1
Mutagenesisi283W → A: Reduces septal localization by a factor of at least 3. 1 Publication1
Mutagenesisi283W → D: Severe localization defects. 1 Publication1
Mutagenesisi285R → A: Reduces septal localization by a factor of at least 3. Binds peptidoglycan poorly. 1 Publication1
Mutagenesisi312C → A: Severely reduces stability of the protein. 1 Publication1
Mutagenesisi313I → A: Reduces septal localization by a factor of at least 3. 1 Publication1

<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_00000873761 – 319Cell division protein FtsNAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi252 ↔ 312UniRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P29131

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

More...PaxDbi		P29131

PRoteomics IDEntifications database

More...PRIDEi		P29131

<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

Interacts with FtsA via its N-terminal cytoplasmic domain (PubMed:22328664, PubMed:24750258, PubMed:25496160, PubMed:25496259).

Interacts with ZapA, FtsQ, FtsW and FtsI (PubMed:17185541, PubMed:20497333).

6 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

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261592, 198 interactors
852725, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1936, Divisome complex

Database of interacting proteins

More...DIPi		DIP-9705N

Protein interaction database and analysis system

More...IntActi		P29131, 24 interactors

Molecular INTeraction database

More...MINTi		P29131

STRING: functional protein association networks

More...STRINGi		511145.b3933

<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

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P29131

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

More...SMRi		P29131

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P29131

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati115 – 1201-16
Repeati145 – 1501-26
Repeati197 – 2002-14
Repeati220 – 2232-24
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini242 – 316SPORUniRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni4 – 6Mediates interaction with FtsAUniRule annotation1 Publication3
Regioni115 – 1502 X 6 AA repeatsAdd BLAST36
Regioni197 – 2232 X 4 AA repeatsAdd BLAST27

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The cytoplasmic region is required for interaction with FtsA (PubMed:24750258). The periplasmic region is composed of a membrane-proximal region containing three short partially formed helices (H1, H2 and H3), followed by an unstructured glutamine-rich linker, and a C-terminal globular SPOR domain (PubMed:15101973, PubMed:19684127). Essential function of FtsN is accomplished by a small region of at most 35 residues that is centered about the H2 helix (PubMed:19684127). The SPOR domain, which exhibits a ribonucleoprotein (RNP) fold, binds peptidoglycan and is a strong septal localization determinant, but it seems not essential for cell division (PubMed:15466024, PubMed:19684127, PubMed:24056104).5 Publications

<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 FtsN family.UniRule annotationCurated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG3087, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_058902_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P29131

Family and domain databases

Database of protein disorder

More...DisProti		DP02271

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.70.1070, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_02039, FtsN_entero, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011930, FtsN
IPR007730, SPOR-like_dom
IPR036680, SPOR-like_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF05036, SPOR, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF110997, SSF110997, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02223, ftsN, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51724, SPOR, 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.

P29131-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQRDYVRRS QPAPSRRKKS TSRKKQRNLP AVSPAMVAIA AAVLVTFIGG 
        60         70         80         90        100
LYFITHHKKE ESETLQSQKV TGNGLPPKPE ERWRYIKELE SRQPGVRAPT 
       110        120        130        140        150
EPSAGGEVKT PEQLTPEQRQ LLEQMQADMR QQPTQLVEVP WNEQTPEQRQ 
       160        170        180        190        200
QTLQRQRQAQ QLAEQQRLAQ QSRTTEQSWQ QQTRTSQAAP VQAQPRQSKP 
       210        220        230        240        250
ASSQQPYQDL LQTPAHTTAQ SKPQQAAPVA RAADAPKPTA EKKDERRWMV 
       260        270        280        290        300
QCGSFRGAEQ AETVRAQLAF EGFDSKITTN NGWNRVVIGP VKGKENADST 
       310 
LNRLKMAGHT NCIRLAAGG
Length:319
Mass (Da):35,793
Last modified:August 29, 2003 - v3
<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:i21CEA5771FF3FB66
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 AAA23935 differs from that shown. Reason: Frameshift.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 conflicti29L → V (PubMed:8509333).Curated1
Sequence conflicti29L → V (Ref. 2) Curated1

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
L14281 Genomic DNA Translation: AAA23814.1
L06547 Genomic DNA Translation: AAA23935.1 Frameshift.
L19201 Genomic DNA Translation: AAB03065.1
U00096 Genomic DNA Translation: AAC76915.1
AP009048 Genomic DNA Translation: BAE77377.1

Protein sequence database of the Protein Information Resource

More...PIRi		S40876

NCBI Reference Sequences

More...RefSeqi		NP_418368.1, NC_000913.3
WP_000068828.1, NZ_SSZK01000014.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76915; AAC76915; b3933
BAE77377; BAE77377; BAE77377

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57732226
948428

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3904
eco:b3933

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.4051

<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
L14281 Genomic DNA Translation: AAA23814.1
L06547 Genomic DNA Translation: AAA23935.1 Frameshift.
L19201 Genomic DNA Translation: AAB03065.1
U00096 Genomic DNA Translation: AAC76915.1
AP009048 Genomic DNA Translation: BAE77377.1
PIRiS40876
RefSeqiNP_418368.1, NC_000913.3
WP_000068828.1, NZ_SSZK01000014.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UTANMR-A243-319[»]
6YN0X-ray2.40B75-93[»]
BMRBiP29131
SMRiP29131
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261592, 198 interactors
852725, 3 interactors
ComplexPortaliCPX-1936, Divisome complex
DIPiDIP-9705N
IntActiP29131, 24 interactors
MINTiP29131
STRINGi511145.b3933

Proteomic databases

jPOSTiP29131
PaxDbiP29131
PRIDEiP29131

Genome annotation databases

EnsemblBacteriaiAAC76915; AAC76915; b3933
BAE77377; BAE77377; BAE77377
GeneIDi57732226
948428
KEGGiecj:JW3904
eco:b3933
PATRICifig|511145.12.peg.4051

Organism-specific databases

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

More...EchoBASEi		EB1491

Phylogenomic databases

eggNOGiCOG3087, Bacteria
HOGENOMiCLU_058902_0_0_6
InParanoidiP29131

Enzyme and pathway databases

BioCyciEcoCyc:EG11529-MONOMER
MetaCyc:EG11529-MONOMER

Miscellaneous databases

EvolutionaryTraceiP29131

Protein Ontology

More...PROi		PR:P29131

Family and domain databases

DisProtiDP02271
Gene3Di3.30.70.1070, 1 hit
HAMAPiMF_02039, FtsN_entero, 1 hit
InterProiView protein in InterPro
IPR011930, FtsN
IPR007730, SPOR-like_dom
IPR036680, SPOR-like_sf
PfamiView protein in Pfam
PF05036, SPOR, 1 hit
SUPFAMiSSF110997, SSF110997, 1 hit
TIGRFAMsiTIGR02223, ftsN, 1 hit
PROSITEiView protein in PROSITE
PS51724, SPOR, 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 nameiFTSN_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: P29131
Secondary accession number(s): Q2M8M9
<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: December 1, 1992
Last sequence update: August 29, 2003
Last modified: April 7, 2021
This is version 176 of the entry and version 3 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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