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Entry version 127 (12 Aug 2020)
Sequence version 1 (06 Dec 2005)
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Protein

Regulator of sigma-E protease RseP

Gene

rseP

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

A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane.6 Publications

Miscellaneous

Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein.

Caution

Was originally thought to be a negative regulator of sigma-E function and to act directly on sigma-E and RpoH; this may not be physiologically relevant.1 Publication

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Inhibited by Zn2+ chelator 1,10-phenanthroline.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi22Zinc; catalyticCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei23Curated1
Metal bindingi26Zinc; catalyticPROSITE-ProRule annotation1

<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

<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

Molecular functionHydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG12436-MONOMER
ECOL316407:JW0171-MONOMER
MetaCyc:EG12436-MONOMER

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M50.004

<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:
Regulator of sigma-E protease RseP (EC:3.4.24.-)
Alternative name(s):
S2P endopeptidase
Site-2 protease RseP
Short name:
S2P protease RseP
Site-2-type intramembrane protease
<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:rseP
Synonyms:ecfE, yaeL
Ordered Locus Names:b0176, JW0171
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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 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>Transmembranei1 – 21HelicalSequence analysisAdd BLAST21
<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 domaini22 – 103Periplasmic1 PublicationAdd BLAST82
Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Topological domaini125 – 375Cytoplasmic1 PublicationAdd BLAST251
Transmembranei376 – 396HelicalSequence analysisAdd BLAST21
Topological domaini397 – 429Periplasmic1 PublicationAdd BLAST33
Transmembranei430 – 450HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

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

Essential. Depletion experiments lead to cessation of growth, elongated cells and limited lysis, as well as decreased amounts of sigma-E. Not essential in an rseA deletion strain, when sigma-E is overexpressed or in ompA-ompC deletion strain. In the latter has severely decreased growth at 20 degrees Celsius. Accumulation of an RseA proteolysis intermediate.6 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>Mutagenesisi22H → A: Loss of protease activity. 6 Publications1
Mutagenesisi22H → F: Loss of protease activity of RseA and signal peptides, does not complement deletion mutant. Binds substrate. 6 Publications1
Mutagenesisi23E → A: Low basal sigma-E activity, sigma-E not induced. No proteolysis of RseA. 3 Publications1
Mutagenesisi23E → D: Behaves like wild-type in vivo, slight reduction in RseA cleavage in vitro. 3 Publications1
Mutagenesisi23E → Q: Does not complement deletion mutant. 3 Publications1
Mutagenesisi23E → S: Loss of protease activity. 3 Publications1
Mutagenesisi26H → F: Does not complement deletion mutant. 1 Publication1
Mutagenesisi115A → V: No effect. Cleaves RseA without previous DegS cleavage; when associated with R-214. 1 Publication1
Mutagenesisi145I → N: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi151L → P: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi162W → R: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi169L → S: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi213L → P: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi214G → E or Q: Cuts RseA without previous DegS cleavage. 2 Publications1
Mutagenesisi214G → R: Weakly cuts RseA without previous DegS cleavage. Stronger cleavage; when associated with V-115. 2 Publications1
Mutagenesisi215I → A: No cleavage of RseA in vitro (PubMed:19706448), cleavage of RseA (PubMed:23016873) in vivo. 2 Publications1
Mutagenesisi234 – 235AA → KK: Cuts RseA without previous DegS cleavage. 1 Publication2
Mutagenesisi243G → Q: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi244D → K: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi246I → Y: Cuts RseA without previous DegS cleavage. 1 Publication1
Mutagenesisi261V → VTDSYTQVASWTEPFPFSIQ GDPRSDQETAFV: Does not complement deletion mutant. 1 Publication1
Mutagenesisi304I → A: No cleavage of RseA in vitro (PubMed:19706448), cleavage of RseA (PubMed:23016873) in vivo. 2 Publications1
Mutagenesisi389N → C, G or L: Decreased substrate binding, retains some proteolytic activity. 1 Publication1
Mutagenesisi389N → Q: No effect. 1 Publication1
Mutagenesisi394N → C: Decreased substrate binding, retains some proteolytic activity. 1 Publication1
Mutagenesisi397P → C: Decreased substrate binding, retains some proteolytic activity. 1 Publication1
Mutagenesisi399P → C: Decreased substrate binding, retains some proteolytic activity. 1 Publication1
Mutagenesisi402D → N: Does not complement deletion mutant, loss of protease activity. 2 Publications1

<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_00000884171 – 450Regulator of sigma-E protease RsePAdd BLAST450

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AEH1

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

More...
PaxDbi
P0AEH1

PRoteomics IDEntifications database

More...
PRIDEi
P0AEH1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Part of the sigma-E regulon. Also has a primary sigma-70 factor promoter.1 Publication

<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 RseA; the third transmembrane domain can be cross-linked to the transmembrane domain of RseA.

2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261736, 104 interactors

Database of interacting proteins

More...
DIPi
DIP-48061N

Protein interaction database and analysis system

More...
IntActi
P0AEH1, 2 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0176

<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

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P0AEH1

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
P0AEH1

<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 <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>Domaini127 – 220PDZ 1PROSITE-ProRule annotationAdd BLAST94
Domaini222 – 309PDZ 2PROSITE-ProRule annotationAdd BLAST88

<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 2 circularly premutated PDZ domains act to negatively regulate protease action on intact RseA; mutations in PDZ 1 (PDZ-N) have a more deleterious effect than similar mutations in PDZ 2 (PDZ-C). A 31 residue insertion in PDZ-C (between Val-261 and Met-262) domain inhibits protease activity, whereas deletion of residues 203-279 alleviates the PDZ-inhibition, allowing cleavage of intact RseA.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 peptidase M50B family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0750, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_025778_0_2_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AEH1

KEGG Orthology (KO)

More...
KOi
K11749

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AEH1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.42.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001478, PDZ
IPR041489, PDZ_6
IPR036034, PDZ_sf
IPR004387, Pept_M50_Zn
IPR008915, Peptidase_M50

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17820, PDZ_6, 1 hit
PF02163, Peptidase_M50, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00228, PDZ, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50156, SSF50156, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00054, TIGR00054, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50106, PDZ, 1 hit
PS00142, ZINC_PROTEASE, 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.

P0AEH1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSFLWDLAS FIVALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR
60 70 80 90 100
RTDKLGTEYV IALIPLGGYV KMLDERAEPV VPELRHHAFN NKSVGQRAAI
110 120 130 140 150
IAAGPVANFI FAIFAYWLVF IIGVPGVRPV VGEIAANSIA AEAQIAPGTE
160 170 180 190 200
LKAVDGIETP DWDAVRLQLV DKIGDESTTI TVAPFGSDQR RDVKLDLRHW
210 220 230 240 250
AFEPDKEDPV SSLGIRPRGP QIEPVLENVQ PNSAASKAGL QAGDRIVKVD
260 270 280 290 300
GQPLTQWVTF VMLVRDNPGK SLALEIERQG SPLSLTLIPE SKPGNGKAIG
310 320 330 340 350
FVGIEPKVIP LPDEYKVVRQ YGPFNAIVEA TDKTWQLMKL TVSMLGKLIT
360 370 380 390 400
GDVKLNNLSG PISIAKGAGM TAELGVVYYL PFLALISVNL GIINLFPLPV
410 420 430 440 450
LDGGHLLFLA IEKIKGGPVS ERVQDFCYRI GSILLVLLMG LALFNDFSRL
Length:450
Mass (Da):49,071
Last modified:December 6, 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:i81A93BC113FBB66C
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
AF407012 Genomic DNA Translation: AAL01378.1
U70214 Genomic DNA Translation: AAB08605.1
U00096 Genomic DNA Translation: AAC73287.1
AP009048 Genomic DNA Translation: BAA77851.1
M11330 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
H64741

NCBI Reference Sequences

More...
RefSeqi
NP_414718.1, NC_000913.3
WP_001295561.1, NZ_STEB01000032.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73287; AAC73287; b0176
BAA77851; BAA77851; BAA77851

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944871

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0171
eco:b0176

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2103

<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
AF407012 Genomic DNA Translation: AAL01378.1
U70214 Genomic DNA Translation: AAB08605.1
U00096 Genomic DNA Translation: AAC73287.1
AP009048 Genomic DNA Translation: BAA77851.1
M11330 Genomic DNA No translation available.
PIRiH64741
RefSeqiNP_414718.1, NC_000913.3
WP_001295561.1, NZ_STEB01000032.1

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
2ZPLX-ray1.70A/B/C127-221[»]
2ZPMX-ray0.98A222-309[»]
3ID1X-ray1.67A127-220[»]
3ID2X-ray3.09A/B222-309[»]
3ID3X-ray2.01A/B222-309[»]
3ID4X-ray1.60A222-307[»]
SMRiP0AEH1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261736, 104 interactors
DIPiDIP-48061N
IntActiP0AEH1, 2 interactors
STRINGi511145.b0176

Protein family/group databases

MEROPSiM50.004

Proteomic databases

jPOSTiP0AEH1
PaxDbiP0AEH1
PRIDEiP0AEH1

Genome annotation databases

EnsemblBacteriaiAAC73287; AAC73287; b0176
BAA77851; BAA77851; BAA77851
GeneIDi944871
KEGGiecj:JW0171
eco:b0176
PATRICifig|1411691.4.peg.2103

Organism-specific databases

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

More...
EchoBASEi
EB2331

Phylogenomic databases

eggNOGiCOG0750, Bacteria
HOGENOMiCLU_025778_0_2_6
InParanoidiP0AEH1
KOiK11749
PhylomeDBiP0AEH1

Enzyme and pathway databases

BioCyciEcoCyc:EG12436-MONOMER
ECOL316407:JW0171-MONOMER
MetaCyc:EG12436-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AEH1

Protein Ontology

More...
PROi
PR:P0AEH1

Family and domain databases

Gene3Di2.30.42.10, 2 hits
InterProiView protein in InterPro
IPR001478, PDZ
IPR041489, PDZ_6
IPR036034, PDZ_sf
IPR004387, Pept_M50_Zn
IPR008915, Peptidase_M50
PfamiView protein in Pfam
PF17820, PDZ_6, 1 hit
PF02163, Peptidase_M50, 1 hit
SMARTiView protein in SMART
SM00228, PDZ, 2 hits
SUPFAMiSSF50156, SSF50156, 2 hits
TIGRFAMsiTIGR00054, TIGR00054, 1 hit
PROSITEiView protein in PROSITE
PS50106, PDZ, 1 hit
PS00142, ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiRSEP_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: P0AEH1
Secondary accession number(s): P37764
<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 6, 2005
Last sequence update: December 6, 2005
Last modified: August 12, 2020
This is version 127 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

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
  3. Peptidase families
    Classification of peptidase families and list of entries
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