Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AEH1

- RSEP_ECOLI

UniProt

P0AEH1 - RSEP_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Regulator of sigma-E protease RseP

Gene

rseP

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Zinc.Curated

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Zinc; catalyticCurated
Active sitei23 – 231Curated
Metal bindingi26 – 261Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. anti-sigma factor antagonist activity Source: EcoCyc
  2. antisigma factor binding Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. metalloendopeptidase activity Source: EcoCyc

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG12436-MONOMER.
ECOL316407:JW0171-MONOMER.
BRENDAi3.4.24.85. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12436. rseP.

Subcellular locationi

Cell inner membrane 4 Publications; Multi-pass membrane protein 4 Publications

GO - Cellular componenti

  1. integral component of plasma membrane Source: EcoliWiki
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221H → A: Loss of protease activity. 6 Publications
Mutagenesisi22 – 221H → F: Loss of protease activity of RseA and signal peptides, does not complement deletion mutant. Binds substrate. 6 Publications
Mutagenesisi23 – 231E → A: Low basal sigma-E activity, sigma-E not induced. No proteolysis of RseA. 3 Publications
Mutagenesisi23 – 231E → D: Behaves like wild-type in vivo, slight reduction in RseA cleavage in vitro. 3 Publications
Mutagenesisi23 – 231E → Q: Does not complement deletion mutant. 3 Publications
Mutagenesisi23 – 231E → S: Loss of protease activity. 3 Publications
Mutagenesisi26 – 261H → F: Does not complement deletion mutant. 1 Publication
Mutagenesisi115 – 1151A → V: No effect. Cleaves RseA without previous DegS cleavage; when associated with R-214. 1 Publication
Mutagenesisi145 – 1451I → N: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi151 – 1511L → P: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi162 – 1621W → R: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi169 – 1691L → S: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi213 – 2131L → P: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi214 – 2141G → E or Q: Cuts RseA without previous DegS cleavage. 2 Publications
Mutagenesisi214 – 2141G → R: Weakly cuts RseA without previous DegS cleavage. Stronger cleavage; when associated with V-115. 2 Publications
Mutagenesisi215 – 2151I → A: No cleavage of RseA in vitro (PubMed:19706448), cleavage of RseA (PubMed:23016873) in vivo. 2 Publications
Mutagenesisi234 – 2352AA → KK: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi243 – 2431G → Q: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi244 – 2441D → K: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi246 – 2461I → Y: Cuts RseA without previous DegS cleavage. 1 Publication
Mutagenesisi261 – 2611V → VTDSYTQVASWTEPFPFSIQ GDPRSDQETAFV: Does not complement deletion mutant. 1 Publication
Mutagenesisi304 – 3041I → A: No cleavage of RseA in vitro (PubMed:19706448), cleavage of RseA (PubMed:23016873) in vivo. 2 Publications
Mutagenesisi389 – 3891N → C, G or L: Decreased substrate binding, retains some proteolytic activity. 1 Publication
Mutagenesisi389 – 3891N → Q: No effect. 1 Publication
Mutagenesisi394 – 3941N → C: Decreased substrate binding, retains some proteolytic activity. 1 Publication
Mutagenesisi397 – 3971P → C: Decreased substrate binding, retains some proteolytic activity. 1 Publication
Mutagenesisi399 – 3991P → C: Decreased substrate binding, retains some proteolytic activity. 1 Publication
Mutagenesisi402 – 4021D → N: Does not complement deletion mutant, loss of protease activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Regulator of sigma-E protease RsePPRO_0000088417Add
BLAST

Proteomic databases

PRIDEiP0AEH1.

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriP0AEH1.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48061N.
IntActiP0AEH1. 1 interaction.
STRINGi511145.b0176.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi130 – 1345
Helixi139 – 1424
Beta strandi150 – 1545
Helixi162 – 17110
Turni172 – 1743
Beta strandi176 – 1838
Beta strandi191 – 1966
Turni204 – 2063
Helixi209 – 2124
Beta strandi215 – 2173
Beta strandi227 – 2293
Beta strandi231 – 2333
Helixi234 – 2374
Beta strandi245 – 2495
Helixi257 – 26610
Beta strandi272 – 2787
Beta strandi281 – 2877
Beta strandi290 – 2923
Beta strandi295 – 2973
Beta strandi299 – 3013
Beta strandi304 – 3074

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 127-307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEH1.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 10382Periplasmic1 PublicationAdd
BLAST
Topological domaini125 – 375251Cytoplasmic1 PublicationAdd
BLAST
Topological domaini397 – 42933Periplasmic1 PublicationAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalSequence AnalysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Transmembranei376 – 39621HelicalSequence AnalysisAdd
BLAST
Transmembranei430 – 45021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini127 – 22094PDZ 1 (PDZ-N)PROSITE-ProRule annotationAdd
BLAST
Domaini222 – 30988PDZ 2 (PDZ-C)PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG0750.
HOGENOMiHOG000006281.
InParanoidiP0AEH1.
KOiK11749.
OMAiPDEYKTV.
OrthoDBiEOG66F07W.
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:
EMBL
GenBank
DDBJ
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.
YP_488478.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73287; AAC73287; b0176.
BAA77851; BAA77851; BAA77851.
GeneIDi12932742.
944871.
KEGGiecj:Y75_p0172.
eco:b0176.
PATRICi32115463. VBIEscCol129921_0183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRi H64741.
RefSeqi NP_414718.1. NC_000913.3.
YP_488478.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZPL X-ray 1.70 A/B/C 127-221 [» ]
2ZPM X-ray 0.98 A 222-309 [» ]
3ID1 X-ray 1.67 A 127-220 [» ]
3ID2 X-ray 3.09 A/B 222-309 [» ]
3ID3 X-ray 2.01 A/B 222-309 [» ]
3ID4 X-ray 1.60 A 222-307 [» ]
ProteinModelPortali P0AEH1.
SMRi P0AEH1. Positions 127-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48061N.
IntActi P0AEH1. 1 interaction.
STRINGi 511145.b0176.

Protein family/group databases

MEROPSi M50.004.

Proteomic databases

PRIDEi P0AEH1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73287 ; AAC73287 ; b0176 .
BAA77851 ; BAA77851 ; BAA77851 .
GeneIDi 12932742.
944871.
KEGGi ecj:Y75_p0172.
eco:b0176.
PATRICi 32115463. VBIEscCol129921_0183.

Organism-specific databases

EchoBASEi EB2331.
EcoGenei EG12436. rseP.

Phylogenomic databases

eggNOGi COG0750.
HOGENOMi HOG000006281.
InParanoidi P0AEH1.
KOi K11749.
OMAi PDEYKTV.
OrthoDBi EOG66F07W.
PhylomeDBi P0AEH1.

Enzyme and pathway databases

BioCyci EcoCyc:EG12436-MONOMER.
ECOL316407:JW0171-MONOMER.
BRENDAi 3.4.24.85. 2026.

Miscellaneous databases

EvolutionaryTracei P0AEH1.
PROi P0AEH1.

Gene expression databases

Genevestigatori P0AEH1.

Family and domain databases

Gene3Di 2.30.42.10. 2 hits.
InterProi IPR001478. PDZ.
IPR004387. Pept_M50_Zn.
IPR008915. Peptidase_M50.
[Graphical view ]
Pfami PF00595. PDZ. 1 hit.
PF02163. Peptidase_M50. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 2 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 2 hits.
TIGRFAMsi TIGR00054. TIGR00054. 1 hit.
PROSITEi PS50106. PDZ. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the Escherichia coli sigma E regulon."
    Dartigalongue C., Missiakas D., Raina S.
    J. Biol. Chem. 276:20866-20875(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Molecular cloning and sequencing of the gene for CDP-diglyceride synthetase of Escherichia coli."
    Icho T., Sparrow C.P., Raetz C.R.H.
    J. Biol. Chem. 260:12078-12083(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
  7. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli."
    Dartigalongue C., Loferer H., Raina S.
    EMBO J. 20:5908-5918(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-22.
  9. "Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli."
    Kanehara K., Akiyama Y., Ito K.
    Gene 281:71-79(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-22; GLU-23; HIS-26; VAL-261 AND ASP-402.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA."
    Kanehara K., Ito K., Akiyama Y.
    Genes Dev. 16:2147-2155(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF RSEA, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-22 AND ASP-402.
    Strain: K12.
  11. "DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response."
    Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.
    Genes Dev. 16:2156-2168(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE CLEAVAGE OF RSEA, POSSIBLE ACTIVE SITE, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-23.
    Strain: K12.
  12. "Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis."
    Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / JM109 / ATCC 53323.
  13. "YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA."
    Kanehara K., Ito K., Akiyama Y.
    EMBO J. 22:6389-6398(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSEA, DOMAIN, MUTAGENESIS OF GLY-214; 234-ALA-ALA-235; GLY-243; ASP-244 AND ILE-246.
    Strain: K12 / AD16.
  14. "RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences."
    Akiyama Y., Kanehara K., Ito K.
    EMBO J. 23:4434-4442(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE CLEAVAGE OF RSEA, MUTAGENESIS OF HIS-22.
  15. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  16. "Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease."
    Koide K., Ito K., Akiyama Y.
    J. Biol. Chem. 283:9562-9570(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF RSEA, INTERACTION WITH RSEA, SUBSTRATE RECOGNITION, MUTAGENESIS OF HIS-22; GLU-23; ASN-389; ASN-394; PRO-397 AND PRO-399.
    Strain: K12 / AD16.
  17. "Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria."
    Saito A., Hizukuri Y., Matsuo E., Chiba S., Mori H., Nishimura O., Ito K., Akiyama Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:13740-13745(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLEAVAGE OF SIGNAL PEPTIDES, ENZYME REGULATION, MUTAGENESIS OF HIS-22.
    Strain: K12.
  18. "PDZ domains of RseP are not essential for sequential cleavage of RseA or stress-induced sigma(E) activation in vivo."
    Hizukuri Y., Akiyama Y.
    Mol. Microbiol. 86:1232-1245(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, DISRUPTION PHENOTYPE, MUTAGENESIS OF ILE-215 AND ILE-304.
    Strain: K12.
  19. "A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli."
    Inaba K., Suzuki M., Maegawa K., Akiyama S., Ito K., Akiyama Y.
    J. Biol. Chem. 283:35042-35052(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 127-221, X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 222-309, FUNCTION IN CLEAVAGE OF RSEA, DOMAIN, MUTAGENESIS OF ALA-115; ILE-145; LEU-151; TRP-162; LEU-169; LEU-213 AND GLY-214.
    Strain: K12.
  20. "Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage."
    Li X., Wang B., Feng L., Kang H., Qi Y., Wang J., Shi Y.
    Proc. Natl. Acad. Sci. U.S.A. 106:14837-14842(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 127-220, X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 222-307, DOMAIN, MUTAGENESIS OF ILE-215 AND ILE-304.

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: October 29, 2014
This is version 87 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

External Data

Dasty 3