RSEA_SALT1
ID RSEA_SALT1 Reviewed; 216 AA.
AC D0ZSY8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Anti-sigma-E factor RseA;
DE AltName: Full=Regulator of SigE;
DE AltName: Full=Sigma-E anti-sigma factor RseA;
DE AltName: Full=Sigma-E factor negative regulatory protein;
GN Name=rseA; OrderedLocusNames=STM14_3233;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP ACTIVITY REGULATION, PROBABLE CLEAVAGE BY DEGS AND RSEP, DISRUPTION
RP PHENOTYPE, AND FUNCTION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19170886; DOI=10.1111/j.1365-2958.2009.06597.x;
RA Muller C., Bang I.S., Velayudhan J., Karlinsey J., Papenfort K., Vogel J.,
RA Fang F.C.;
RT "Acid stress activation of the sigma(E) stress response in Salmonella
RT enterica serovar Typhimurium.";
RL Mol. Microbiol. 71:1228-1238(2009).
CC -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive
CC form by an anti-sigma factor until released by regulated intramembrane
CC proteolysis (RIP). RIP occurs when an extracytoplasmic signal
CC (periplasmic or acid stress or heat shock) triggers a concerted
CC proteolytic cascade to transmit information and elicit cellular
CC responses. The membrane-spanning regulatory substrate protein is first
CC cut periplasmically (site-1 protease, S1P, DegS), then within the
CC membrane itself (site-2 protease, S2P, RseP), while cytoplasmic
CC proteases finish degrading the anti-sigma factor, liberating sigma-E
CC (Probable). In this organism acid stress response does not require DegS
CC degradation. {ECO:0000269|PubMed:19170886, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Responds differently to heat shock versus acid
CC shock; degradation in response to heat shock requires sequential DegS
CC and RseP action, whereas degradation in response to acid shock requires
CC only RseP. {ECO:0000269|PubMed:19170886}.
CC -!- SUBUNIT: Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); this
CC inhibits the interaction of sigma-E with the RNA polymerase catalytic
CC core and leads to a decreased expression of sigma-E-regulated genes.
CC Interacts with RseB (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
CC -!- PTM: Sequentially cleaved by DegS (a site-1 protease) in its
CC periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2
CC protease) between positions Ala-108 and Cys-109. The N-terminal
CC fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent
CC fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE
CC from RseA (Probable). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Derepression and constitutive activation of
CC sigma-E function, consequently loss of acid stress response.
CC {ECO:0000269|PubMed:19170886}.
CC -!- SIMILARITY: Belongs to the RseA family. {ECO:0000305}.
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DR EMBL; CP001363; ACY89662.1; -; Genomic_DNA.
DR RefSeq; WP_001168374.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZSY8; -.
DR SMR; D0ZSY8; -.
DR EnsemblBacteria; ACY89662; ACY89662; STM14_3233.
DR KEGG; seo:STM14_3233; -.
DR PATRIC; fig|588858.6.peg.3000; -.
DR HOGENOM; CLU_108851_1_0_6; -.
DR OMA; PEWNIAE; -.
DR BioCyc; SENT588858:STM14_RS14450-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
DR GO; GO:0097533; P:cellular stress response to acid chemical; IMP:UniProtKB.
DR CDD; cd16328; RseA_N; 1.
DR Gene3D; 1.10.10.880; -; 1.
DR InterPro; IPR005573; Anti-sigma_E_RseA_C.
DR InterPro; IPR005572; Anti-sigma_E_RseA_N.
DR InterPro; IPR036147; Anti-sigma_E_RseA_N_sf.
DR InterPro; IPR026279; RseA.
DR Pfam; PF03873; RseA_C; 1.
DR Pfam; PF03872; RseA_N; 1.
DR PIRSF; PIRSF016938; RseA; 1.
DR SUPFAM; SSF89069; SSF89069; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Coiled coil; Membrane; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..216
FT /note="Anti-sigma-E factor RseA"
FT /id="PRO_0000424884"
FT TOPO_DOM 1..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..121
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..216
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..202
FT /evidence="ECO:0000255"
FT SITE 108..109
FT /note="Cleavage; by RseP"
FT /evidence="ECO:0000250"
FT SITE 148..149
FT /note="Cleavage; by DegS"
FT /evidence="ECO:0000250"
SQ 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
