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Protein

Anti-sigma-E factor RseA

Gene

rseA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E. Overexpression of RseA blocks sigma-E from acting, results in cell lysis in stationary phase and temperature-sensitivity above 37 degrees Celsius.3 Publications

GO - Molecular functioni

  • sigma factor antagonist activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG12341-MONOMER.
ECOL316407:JW2556-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Anti-sigma-E factor RseA
Alternative name(s):
Regulator of SigE
Sigma-E anti-sigma factor RseA
Sigma-E factor negative regulatory protein
Gene namesi
Name:rseA
Synonyms:mclA, yfiJ
Ordered Locus Names:b2572, JW2556
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12341. rseA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 100Cytoplasmic1 PublicationAdd BLAST100
Transmembranei101 – 118Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST18
Topological domaini119 – 216Periplasmic1 PublicationAdd BLAST98

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

About 10-fold increased sigma-E activity. Neither sigma-E nor RseB associate with the inner membrane.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 28Missing : Loss of anti-sigma factor activity. 1 PublicationAdd BLAST28
Mutagenesisi11D → H: Loss of anti-sigma factor activity. 1 Publication1
Mutagenesisi19L → P: Loss of anti-sigma factor activity. 1 Publication1
Mutagenesisi33W → C: Loss of anti-sigma factor activity. 1 Publication1
Mutagenesisi79Q → A: No binding of N-terminal fragment to SspB. 1 Publication1
Mutagenesisi85W → A: No binding of N-terminal fragment to SspB. 1 Publication1
Mutagenesisi88M → A: Reduced binding of N-terminal fragment to SspB. 1 Publication1
Mutagenesisi107 – 108AA → DD: Significantly less degradation by ClpX-ClpP when present as a 1-108 peptide fragment. 1 Publication2
Mutagenesisi146S → X: No effect on protein cleavage. 1 Publication1
Mutagenesisi147P → X: No effect on protein cleavage in vitro and in vivo. 2 Publications1
Mutagenesisi148V → A, C, I, L, M, N or T: Normal cleavage by DegS and RseP in vitro (PubMed:19706448), for A-148 decreased cleavage by DegS in vivo (PubMed:23016873). 2 Publications1
Mutagenesisi148V → D, E, G, F or P: Not cleaved by DegS nor RseP in vitro (PubMed:19706448). 2 Publications1
Mutagenesisi148V → H, K, Q, R, S or Y: Cleaved by DegS but not by RseP in vitro (PubMed:19706448), for R-148 and S-148 decreased cleavage by DegS in vivo (PubMed:23016873). 2 Publications1
Mutagenesisi162 – 169QQQQVQEQ → AAAAVAEA: RseA is degraded by RseP in the absence of DegS. 1 Publication8
Mutagenesisi172R → A: Still binds RseB. No binding to RseB; when associated with A-185. 1 Publication1
Mutagenesisi172R → D: No binding to RseB. 1 Publication1
Mutagenesisi185R → A: Still binds RseB. No binding to RseB; when associated with A-172. 1 Publication1
Mutagenesisi185R → E: No binding to RseB. 1 Publication1
Mutagenesisi190 – 200QLQFEQAQTQQ → ALAFFAAATAA: RseA is degraded by RseP in the absence of DegS. 1 PublicationAdd BLAST11

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000974801 – 216Anti-sigma-E factor RseAAdd BLAST216

Post-translational modificationi

Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2 protease) between positions Ala-108 and Cys-109. The N-terminal fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE from RseA.10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei108 – 109Cleavage; by RseP2
Sitei148 – 149Cleavage; by DegS2

Proteomic databases

PaxDbiP0AFX7.
PRIDEiP0AFX7.

Expressioni

Inductioni

Transiently induced by cold shock in a PNPase-dependent fashion. Upon stress induction (OMPs or heat shock) decreases in under 3 minutes (at protein level). Part of the rpoE-rseA-rseB-rseC operon.2 Publications

Interactioni

Subunit structurei

Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); this inhibits the interaction of sigma-E with the RNA polymerase catalytic core and leads to a decreased expression of sigma-E-regulated genes. Interacts with RseB with 1:1 stoichiometry. The liberated N-terminus (residues 1-108) forms a complex with SspB and RpoE; binding to SspB is competitively inhibited by ssrA-tags, although the 2 proteins bind in opposite directions in SspB's peptide-binding groove.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
degSP0AEE34EBI-1117560,EBI-1132101
rseBP0AFX96EBI-1117560,EBI-1135231

Protein-protein interaction databases

DIPiDIP-39581N.
IntActiP0AFX7. 5 interactors.
STRINGi511145.b2572.

Structurei

Secondary structure

1216
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Helixi17 – 24Combined sources8
Helixi27 – 44Combined sources18
Beta strandi49 – 53Combined sources5
Helixi55 – 64Combined sources10
Helixi82 – 85Combined sources4
Helixi89 – 93Combined sources5
Helixi134 – 136Combined sources3
Helixi170 – 186Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OR7X-ray2.00C/F1-90[»]
1YFNX-ray1.80E/F/G/H77-108[»]
3M4WX-ray2.30E/F/G/H121-216[»]
DisProtiDP00552.
ProteinModelPortaliP0AFX7.
SMRiP0AFX7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFX7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 97Sufficient to repress sigma-EAdd BLAST97
Regioni169 – 186Primary binding site for RseBAdd BLAST18
Regioni190 – 200Poly-Gln (Q2)Add BLAST11

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili158 – 202Sequence analysisAdd BLAST45

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi162 – 169Poly-Gln (Q1)8

Domaini

The N-terminal cytosolic domain interacts with sigma-E, and upon overexpression leads to temperature sensitivity above 37 degrees Celsius and cell lysis in stationary phase. After degradation by RseP residues 77-108 bind to SspB, targeting RseA for degradation by the ClpX-ClpP protease.
The C-terminal periplasmic domain (residues 169-186) interacts with RseB and is also the target for DegS; RseB and DegS binding sites do not appreciably overlap. Gln-rich regions (residues 162-169, Q1, and 190-200, Q2) contribute to preventing RseP from acting before DegS. Insertion of 8 consecutive Gln residues into a protein lacking Q1 and Q2 restores DegS-depenedence of RseP cleavage.

Sequence similaritiesi

Belongs to the RseA family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG41069PW. Bacteria.
COG3073. LUCA.
HOGENOMiHOG000272262.
InParanoidiP0AFX7.
KOiK03597.
OMAiGVQHYNQ.

Family and domain databases

InterProiIPR005573. Anti-sigma_E_RseA_C.
IPR005572. Anti-sigma_E_RseA_N.
IPR026279. RseA.
[Graphical view]
PfamiPF03873. RseA_C. 1 hit.
PF03872. RseA_N. 1 hit.
[Graphical view]
PIRSFiPIRSF016938. RseA. 1 hit.
SUPFAMiSSF89069. SSF89069. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKEQLSALM DGETLDSELL NELAHNPEMQ KTWESYHLIR DSMRGDTPEV
60 70 80 90 100
LHFDISSRVM AAIEEEPVRQ PATLIPEAQP APHQWQKMPF WQKVRPWAAQ
110 120 130 140 150
LTQMGVAACV SLAVIVGVQH YNGQSETSQQ PETPVFNTLP MMGKASPVSL
160 170 180 190 200
GVPSEATANN GQQQQVQEQR RRINAMLQDY ELQRRLHSEQ LQFEQAQTQQ
210
AAVQVPGIQT LGTQSQ
Length:216
Mass (Da):24,321
Last modified:December 20, 2005 - v1
Checksum:i63BD12131C611C32
GO

Sequence cautioni

The sequence D13169 differs from that shown. Reason: Frameshift at position 75.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10148 Genomic DNA. Translation: AAA83999.1.
U37089 Genomic DNA. Translation: AAC45315.1.
D64044 Genomic DNA. Translation: BAA10919.1.
D13169 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75625.1.
AP009048 Genomic DNA. Translation: BAE76748.1.
U37455 Genomic DNA. Translation: AAC45318.1.
PIRiB57255.
RefSeqiNP_417067.1. NC_000913.3.
WP_001168459.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75625; AAC75625; b2572.
BAE76748; BAE76748; BAE76748.
GeneIDi947053.
KEGGiecj:JW2556.
eco:b2572.
PATRICi32120543. VBIEscCol129921_2674.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10148 Genomic DNA. Translation: AAA83999.1.
U37089 Genomic DNA. Translation: AAC45315.1.
D64044 Genomic DNA. Translation: BAA10919.1.
D13169 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75625.1.
AP009048 Genomic DNA. Translation: BAE76748.1.
U37455 Genomic DNA. Translation: AAC45318.1.
PIRiB57255.
RefSeqiNP_417067.1. NC_000913.3.
WP_001168459.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OR7X-ray2.00C/F1-90[»]
1YFNX-ray1.80E/F/G/H77-108[»]
3M4WX-ray2.30E/F/G/H121-216[»]
DisProtiDP00552.
ProteinModelPortaliP0AFX7.
SMRiP0AFX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39581N.
IntActiP0AFX7. 5 interactors.
STRINGi511145.b2572.

Proteomic databases

PaxDbiP0AFX7.
PRIDEiP0AFX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75625; AAC75625; b2572.
BAE76748; BAE76748; BAE76748.
GeneIDi947053.
KEGGiecj:JW2556.
eco:b2572.
PATRICi32120543. VBIEscCol129921_2674.

Organism-specific databases

EchoBASEiEB2245.
EcoGeneiEG12341. rseA.

Phylogenomic databases

eggNOGiENOG41069PW. Bacteria.
COG3073. LUCA.
HOGENOMiHOG000272262.
InParanoidiP0AFX7.
KOiK03597.
OMAiGVQHYNQ.

Enzyme and pathway databases

BioCyciEcoCyc:EG12341-MONOMER.
ECOL316407:JW2556-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFX7.
PROiP0AFX7.

Family and domain databases

InterProiIPR005573. Anti-sigma_E_RseA_C.
IPR005572. Anti-sigma_E_RseA_N.
IPR026279. RseA.
[Graphical view]
PfamiPF03873. RseA_C. 1 hit.
PF03872. RseA_N. 1 hit.
[Graphical view]
PIRSFiPIRSF016938. RseA. 1 hit.
SUPFAMiSSF89069. SSF89069. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRSEA_ECOLI
AccessioniPrimary (citable) accession number: P0AFX7
Secondary accession number(s): P38106, Q2MAF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

PubMed:9159522 mis-identifies Trp-33 as residue 32.Curated
In vitro (PubMed:19706448) and in vivo (PubMed:23016873) results on the importance of the identity of residue 148 for cleavage by RseP differ.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. 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.