Regulator of sigma E protease - Escherichia coli (strain K12)

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P0AEH1 (RSEP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Regulator of sigma E protease
EC=3.4.24.-

Gene names

Name:	rseP
Synonyms:	ecfE, yaeL
Ordered Locus Names:	b0176, JW0171

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma E (RpoE) activity through the proteolysis of RseA. In vitro, can also cleave sequences in transmembrane regions of other proteins as well as the signal sequence of beta-lactamase. Purified RseP was also shown to degrade RpoH and RpoE in vitro. Ref.8 Ref.9 Ref.11
Cofactor	Zinc Probable.
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.10 Ref.12.
Domain	The PDZ domain is required for the inhibitory reaction that prevents cleavage of intact RseA.
Sequence similarities	Belongs to the peptidase M50B family. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from mutant phenotype PubMed 12183368 Ref.9. Source: EcoCyc
Cellular_component	integral to plasma membrane Inferred from direct assay Ref.10. Source: EcoliWiki
Molecular_function	anti-sigma factor antagonist activity Inferred from mutant phenotype PubMed 12183368 Ref.9. Source: EcoCyc antisigma factor binding Inferred from direct assay PubMed 19706448. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from direct assay PubMed 19706448. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Regulator of sigma E protease

PRO_0000088417

Regions

Transmembrane

107 – 127

Helical; Potential

Transmembrane

376 – 396

Helical; Potential

Transmembrane

430 – 450

Helical; Potential

Domain

199 – 291

PDZ

Sites

Active site

Potential

Metal binding

Zinc; catalytic Probable

Metal binding

Zinc; catalytic Potential

Experimental info

Mutagenesis

H → A or F: Loss of activity. Ref.8 Ref.11

Secondary structure

450

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEH1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 81A93BC113FBB66C
Show »

FASTA

450

49,071

        10         20         30         40         50         60 
MLSFLWDLAS FIVALGVLIT VHEFGHFWVA RRCGVRVERF SIGFGKALWR RTDKLGTEYV 

        70         80         90        100        110        120 
IALIPLGGYV KMLDERAEPV VPELRHHAFN NKSVGQRAAI IAAGPVANFI FAIFAYWLVF 

       130        140        150        160        170        180 
IIGVPGVRPV VGEIAANSIA AEAQIAPGTE LKAVDGIETP DWDAVRLQLV DKIGDESTTI 

       190        200        210        220        230        240 
TVAPFGSDQR RDVKLDLRHW AFEPDKEDPV SSLGIRPRGP QIEPVLENVQ PNSAASKAGL 

       250        260        270        280        290        300 
QAGDRIVKVD GQPLTQWVTF VMLVRDNPGK SLALEIERQG SPLSLTLIPE SKPGNGKAIG 

       310        320        330        340        350        360 
FVGIEPKVIP LPDEYKVVRQ YGPFNAIVEA TDKTWQLMKL TVSMLGKLIT GDVKLNNLSG 

       370        380        390        400        410        420 
PISIAKGAGM TAELGVVYYL PFLALISVNL GIINLFPLPV LDGGHLLFLA IEKIKGGPVS 

       430        440        450 
ERVQDFCYRI GSILLVLLMG LALFNDFSRL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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].
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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: ROLE IN DEGRADATION OF RPOE AND RPOH, MUTAGENESIS OF HIS-22.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

H64741.

RefSeq

NP_414718.1. NC_000913.2.
YP_488478.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AEH1.

SMR

P0AEH1. Positions 127-219, 222-307.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48061N.

IntAct

P0AEH1. 1 interaction.

STRING

511145.b0176.

Protein family/group databases

MEROPS

M50.004.

Proteomic databases

PRIDE

P0AEH1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73287; AAC73287; b0176.
BAA77851; BAA77851; BAA77851.

GeneID

12932742.
944871.

KEGG

ecj:Y75_p0172.
eco:b0176.

PATRIC

32115463. VBIEscCol129921_0183.

Organism-specific databases

EchoBASE

EB2331.

EcoGene

EG12436. rseP.

Phylogenomic databases

eggNOG

COG0750.

HOGENOM

HOG000006281.

K11749.

OMA

PDEYKTV.

ProtClustDB

PRK10779.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12436-MONOMER.
ECOL316407:JW0171-MONOMER.

BRENDA

3.4.24.85. 2026.

Gene expression databases

Genevestigator

P0AEH1.

Family and domain databases

InterPro

IPR001478. PDZ.
IPR004387. Pept_M50_Zn.
IPR008915. Peptidase_M50.
[Graphical view]

Pfam

PF00595. PDZ. 1 hit.
PF02163. Peptidase_M50. 1 hit.
[Graphical view]

SMART

SM00228. PDZ. 2 hits.
[Graphical view]

SUPFAM

SSF50156. PDZ. 2 hits.

TIGRFAMs

TIGR00054. TIGR00054. 1 hit.

PROSITE

PS50106. PDZ. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AEH1.

Entry information

Entry name

RSEP_ECOLI

Accession

Primary (citable) accession number: P0AEH1
Secondary accession number(s): P37764

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents