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P44791 (RSEA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:rseA
Synonyms:mclA
Ordered Locus Names:HI_0629
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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 forms a complex with SspB and RpoE By similarity.

Subcellular location

Cell inner membrane; Single-pass type II membrane protein By similarity. Note: Following cleavage by DegS the large fragment of the protein is still in the inner membrane and retains its anti-sigma-E activity By similarity.

Domain

The N-terminal cytosolic domain interacts with sigma-E. After degradation by RseP binds to SspB, targeting RseA for degradation by the ClpX-ClpP protease By similarity.

The C-terminal periplasmic domain interacts with RseB and is also the target for DegS By similarity.

Post-translational modification

Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-147 and Ser-148, then by RseP (a site-2 protease). 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 By similarity.

Sequence similarities

Belongs to the RseA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 195195Anti-sigma-E factor RseA
PRO_0000097482

Regions

Topological domain1 – 9494Cytoplasmic Potential
Transmembrane95 – 11723Helical; Signal-anchor for type II membrane protein; Potential
Topological domain118 – 19578Periplasmic Potential
Coiled coil160 – 18122 Potential

Sites

Site148 – 1492Cleavage; by DegS By similarity

Sequences

Sequence LengthMass (Da)Tools
P44791 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 9BA4C6AA8F91CA0F

FASTA19521,733
        10         20         30         40         50         60 
MQKEQLSAYM DGEQVETDLI DALLRDEELQ ASWHSFHTVR SVMRKESAVF LGADFTAKMA 

        70         80         90        100        110        120 
DLIELEDVKK VDVIAVSQPE PEDAHNSVFM QKLKAFFAPM TQVAVAAGVC LVAVLGVQSF 

       130        140        150        160        170        180 
NNKNDASNLP ETPVLQTLPF NNAVQEVSYN APSKDTLTSD QLEKKSRRIG AMLQNYELQR 

       190 
RMHSDALDVS SSQVR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22289.1.
PIRG64082.
RefSeqNP_438789.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44791.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22289; AAC22289; HI_0629.
GeneID949684.
KEGGhin:HI0629.
PATRIC20189853. VBIHaeInf48452_0655.

Phylogenomic databases

eggNOGCOG3073.
KOK03597.
OMAFILANFP.
OrthoDBEOG6V7BSG.
PhylomeDBP44791.

Family and domain databases

InterProIPR005573. Anti-sigma_E_RseA_C.
IPR005572. Anti-sigma_E_RseA_N.
IPR026279. RseA.
[Graphical view]
PfamPF03873. RseA_C. 1 hit.
PF03872. RseA_N. 1 hit.
[Graphical view]
PIRSFPIRSF016938. RseA. 1 hit.
SUPFAMSSF89069. SSF89069. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRSEA_HAEIN
AccessionPrimary (citable) accession number: P44791
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names