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Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein)

 RSEA_SALT1              Reviewed;         216 AA.
D0ZSY8;
22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 1.
12-SEP-2018, entry version 43.
RecName: Full=Anti-sigma-E factor RseA;
AltName: Full=Regulator of SigE;
AltName: Full=Sigma-E anti-sigma factor RseA;
AltName: Full=Sigma-E factor negative regulatory protein;
Name=rseA; OrderedLocusNames=STM14_3233;
Salmonella typhimurium (strain 14028s / SGSC 2262).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=588858;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=14028s / SGSC 2262;
PubMed=19897643; DOI=10.1128/JB.01233-09;
Jarvik T., Smillie C., Groisman E.A., Ochman H.;
"Short-term signatures of evolutionary change in the Salmonella
enterica serovar typhimurium 14028 genome.";
J. Bacteriol. 192:560-567(2010).
[2]
ACTIVITY REGULATION, PROBABLE CLEAVAGE BY DEGS AND RSEP, DISRUPTION
PHENOTYPE, AND FUNCTION.
STRAIN=14028s / SGSC 2262;
PubMed=19170886; DOI=10.1111/j.1365-2958.2009.06597.x;
Muller C., Bang I.S., Velayudhan J., Karlinsey J., Papenfort K.,
Vogel J., Fang F.C.;
"Acid stress activation of the sigma(E) stress response in Salmonella
enterica serovar Typhimurium.";
Mol. Microbiol. 71:1228-1238(2009).
-!- 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 (periplasmic or acid stress or heat shock)
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 (Probable). In this organism acid
stress response does not require DegS degradation.
{ECO:0000269|PubMed:19170886, ECO:0000305}.
-!- ACTIVITY REGULATION: Responds differently to heat shock versus
acid shock; degradation in response to heat shock requires
sequential DegS and RseP action, whereas degradation in response
to acid shock requires only RseP. {ECO:0000269|PubMed:19170886}.
-!- SUBUNIT: 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 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-
pass type II membrane protein {ECO:0000250}.
-!- PTM: 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 (Probable). {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Derepression and constitutive activation of
sigma-E function, consequently loss of acid stress response.
{ECO:0000269|PubMed:19170886}.
-!- SIMILARITY: Belongs to the RseA family. {ECO:0000305}.
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EMBL; CP001363; ACY89662.1; -; Genomic_DNA.
RefSeq; WP_001168374.1; NC_016856.1.
ProteinModelPortal; D0ZSY8; -.
SMR; D0ZSY8; -.
EnsemblBacteria; ACY89662; ACY89662; STM14_3233.
KEGG; seo:STM14_3233; -.
PATRIC; fig|588858.6.peg.3000; -.
KO; K03597; -.
OMA; GVQHYNQ; -.
OrthoDB; POG091H05JT; -.
Proteomes; UP000002695; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
GO; GO:0097533; P:cellular stress response to acid chemical; IMP:UniProtKB.
CDD; cd16328; RseA_N; 1.
Gene3D; 1.10.10.880; -; 1.
InterPro; IPR005573; Anti-sigma_E_RseA_C.
InterPro; IPR005572; Anti-sigma_E_RseA_N.
InterPro; IPR036147; Anti-sigma_E_RseA_N_sf.
InterPro; IPR026279; RseA.
Pfam; PF03873; RseA_C; 1.
Pfam; PF03872; RseA_N; 1.
PIRSF; PIRSF016938; RseA; 1.
SUPFAM; SSF89069; SSF89069; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Coiled coil; Complete proteome;
Membrane; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 216 Anti-sigma-E factor RseA.
/FTId=PRO_0000424884.
TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 121 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 122 216 Periplasmic. {ECO:0000255}.
COILED 161 202 {ECO:0000255}.
COMPBIAS 162 216 Gln-rich.
SITE 108 109 Cleavage; by RseP. {ECO:0000250}.
SITE 148 149 Cleavage; by DegS. {ECO:0000250}.
SEQUENCE 216 AA; 24223 MW; 66E1BF61BD7EDC87 CRC64;
MQKEKLSALM DGETLDSELL KALTHDPEMQ KTWESYHLIR DSMRGDTPDV LHFDISARVM
AAIENEPVRQ VSPLIPEAQP APQQWQKMPF WKKVRPWAAQ LTQMGVAACV SLAVIVGVQH
YNGQSETSQQ PETPVFNTLP MMGKASPVSL GVPSEAAPVG SQQQQVQEQR RRINAMLQDY
ELQRRLHSEQ LQFEQAQTQQ AAVQVPGIQT LGTQSQ


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