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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-Experimental evidence at protein leveli

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

Cofactori

Zn2+Curated

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi22Zinc; catalyticCurated1
Active sitei23Curated1
Metal bindingi26Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • anti-sigma factor antagonist activity Source: EcoCyc
  • antisigma factor binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG12436-MONOMER.
ECOL316407:JW0171-MONOMER.

Protein family/group databases

MEROPSiM50.004.

Names & Taxonomyi

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
Gene namesi
Name:rseP
Synonyms:ecfE, yaeL
Ordered Locus Names:b0176, JW0171
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12436. rseP.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei1 – 21HelicalSequence analysisAdd BLAST21
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

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

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
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000884171 – 450Regulator of sigma-E protease RsePAdd BLAST450

Proteomic databases

EPDiP0AEH1.
PaxDbiP0AEH1.
PRIDEiP0AEH1.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Interacts with RseA; the third transmembrane domain can be cross-linked to the transmembrane domain of RseA.2 Publications

GO - Molecular functioni

  • antisigma factor binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261736. 75 interactors.
DIPiDIP-48061N.
IntActiP0AEH1. 1 interactor.
STRINGi511145.b0176.

Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi130 – 134Combined sources5
Helixi139 – 142Combined sources4
Beta strandi150 – 154Combined sources5
Helixi162 – 171Combined sources10
Turni172 – 174Combined sources3
Beta strandi176 – 183Combined sources8
Beta strandi191 – 196Combined sources6
Turni204 – 206Combined sources3
Helixi209 – 212Combined sources4
Beta strandi215 – 217Combined sources3
Beta strandi227 – 229Combined sources3
Beta strandi231 – 233Combined sources3
Helixi234 – 237Combined sources4
Beta strandi245 – 249Combined sources5
Helixi257 – 266Combined sources10
Beta strandi272 – 278Combined sources7
Beta strandi281 – 287Combined sources7
Beta strandi290 – 292Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi304 – 307Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP0AEH1.
SMRiP0AEH1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEH1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini127 – 220PDZ 1 (PDZ-N)PROSITE-ProRule annotationAdd BLAST94
Domaini222 – 309PDZ 2 (PDZ-C)PROSITE-ProRule annotationAdd BLAST88

Domaini

The 2 circularly premutated PDZ domains act to negatively regulate protease action on intact RseA; mutations in PDZ-N have a more deleterious effect than similar mutations in 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

Sequence similaritiesi

Belongs to the peptidase M50B family.Curated
Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DZP. Bacteria.
COG0750. LUCA.
HOGENOMiHOG000006281.
InParanoidiP0AEH1.
KOiK11749.
OMAiQMIVGKR.
PhylomeDBiP0AEH1.

Family and domain databases

Gene3Di2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR004387. Pept_M50_Zn.
IPR008915. Peptidase_M50.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF02163. Peptidase_M50. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
TIGRFAMsiTIGR00054. TIGR00054. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i81A93BC113FBB66C
GO

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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73287; AAC73287; b0176.
BAA77851; BAA77851; BAA77851.
GeneIDi944871.
KEGGiecj:JW0171.
eco:b0176.
PATRICi32115463. VBIEscCol129921_0183.

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_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP0AEH1.
SMRiP0AEH1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261736. 75 interactors.
DIPiDIP-48061N.
IntActiP0AEH1. 1 interactor.
STRINGi511145.b0176.

Protein family/group databases

MEROPSiM50.004.

Proteomic databases

EPDiP0AEH1.
PaxDbiP0AEH1.
PRIDEiP0AEH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73287; AAC73287; b0176.
BAA77851; BAA77851; BAA77851.
GeneIDi944871.
KEGGiecj:JW0171.
eco:b0176.
PATRICi32115463. VBIEscCol129921_0183.

Organism-specific databases

EchoBASEiEB2331.
EcoGeneiEG12436. rseP.

Phylogenomic databases

eggNOGiENOG4105DZP. Bacteria.
COG0750. LUCA.
HOGENOMiHOG000006281.
InParanoidiP0AEH1.
KOiK11749.
OMAiQMIVGKR.
PhylomeDBiP0AEH1.

Enzyme and pathway databases

BioCyciEcoCyc:EG12436-MONOMER.
ECOL316407:JW0171-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEH1.
PROiP0AEH1.

Family and domain databases

Gene3Di2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR004387. Pept_M50_Zn.
IPR008915. Peptidase_M50.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF02163. Peptidase_M50. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 2 hits.
TIGRFAMsiTIGR00054. TIGR00054. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRSEP_ECOLI
AccessioniPrimary (citable) accession number: P0AEH1
Secondary accession number(s): P37764
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.