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P0AEH1

- RSEP_ECOLI

UniProt

P0AEH1 - RSEP_ECOLI

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
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    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

    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

    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.
    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.
    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

    MLSFLWDLAS FIVALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR    50
    RTDKLGTEYV IALIPLGGYV KMLDERAEPV VPELRHHAFN NKSVGQRAAI 100
    IAAGPVANFI FAIFAYWLVF IIGVPGVRPV VGEIAANSIA AEAQIAPGTE 150
    LKAVDGIETP DWDAVRLQLV DKIGDESTTI TVAPFGSDQR RDVKLDLRHW 200
    AFEPDKEDPV SSLGIRPRGP QIEPVLENVQ PNSAASKAGL QAGDRIVKVD 250
    GQPLTQWVTF VMLVRDNPGK SLALEIERQG SPLSLTLIPE SKPGNGKAIG 300
    FVGIEPKVIP LPDEYKVVRQ YGPFNAIVEA TDKTWQLMKL TVSMLGKLIT 350
    GDVKLNNLSG PISIAKGAGM TAELGVVYYL PFLALISVNL GIINLFPLPV 400
    LDGGHLLFLA IEKIKGGPVS ERVQDFCYRI GSILLVLLMG LALFNDFSRL 450
    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.
    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

    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 1, 2014
    This is version 86 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