P44791 (RSEA_HAEIN) Reviewed, UniProtKB/Swiss-Prot
Last modified July 9, 2014. Version 79. History...
Names and origin
|Protein names||Recommended name:|
Anti-sigma-E factor RseA
Regulator of SigE
Sigma-E anti-sigma factor RseA
Sigma-E factor negative regulatory protein
|Organism||Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]|
|Taxonomic identifier||71421 [NCBI]|
|Taxonomic lineage||Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›|
|Sequence length||195 AA.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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.
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.
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.
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.
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.
Belongs to the RseA family.
|Cellular component||Cell inner membrane|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Biological_process||regulation of transcription, DNA-templated|
Inferred from electronic annotation. Source: UniProtKB-KWresponse to stress
Inferred from electronic annotation. Source: InterProtranscription, DNA-templated
Inferred from electronic annotation. Source: UniProtKB-KW
|Cellular_component||integral component of membrane|
Inferred from electronic annotation. Source: UniProtKB-KWplasma membrane
Inferred from electronic annotation. Source: UniProtKB-SubCell
|Molecular_function||sigma factor antagonist activity|
Inferred from electronic annotation. Source: InterPro
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 195||195||Anti-sigma-E factor RseA||PRO_0000097482|
|Topological domain||1 – 94||94||Cytoplasmic Potential|
|Transmembrane||95 – 117||23||Helical; Signal-anchor for type II membrane protein; Potential|
|Topological domain||118 – 195||78||Periplasmic Potential|
|Coiled coil||160 – 181||22||Potential|
|Site||148 – 149||2||Cleavage; by DegS By similarity|
|||"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."|
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
|L42023 Genomic DNA. Translation: AAC22289.1.|
|RefSeq||NP_438789.1. NC_000907.1. |
3D structure databases
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|EnsemblBacteria||AAC22289; AAC22289; HI_0629. |
|PATRIC||20189853. VBIHaeInf48452_0655. |
Family and domain databases
|InterPro||IPR005573. Anti-sigma_E_RseA_C. |
|Pfam||PF03873. RseA_C. 1 hit. |
PF03872. RseA_N. 1 hit.
|PIRSF||PIRSF016938. RseA. 1 hit. |
|SUPFAM||SSF89069. SSF89069. 1 hit. |
|Accession||Primary (citable) accession number: P44791|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Prokaryotic Protein Annotation Program|