RSEB_SALT1
ID RSEB_SALT1 Reviewed; 318 AA.
AC D0ZSY7;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Sigma-E factor regulatory protein RseB;
DE Flags: Precursor;
GN Name=rseB; OrderedLocusNames=STM14_3232;
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 DISRUPTION PHENOTYPE.
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: Negatively modulates the activity of sigma-E (RpoE) by
CC stabilizing RseA under non-stress conditions. Although not essential
CC for association of sigma-E with Rsea it increases their affinity 2- to
CC 3-fold. When bound to RseA it prevents proteolysis by DegS, which is
CC probably relieved by lipopolysaccharide binding (LPS) (By similarity).
CC {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Binding to RseA is inhibited by LPS fragments;
CC phosphorylated N-acetylglucosamine (GlcNAc) with N-linked acyl chains
CC are minimally necessary to disrupt binding to RseA. Once RseB is no
CC longer bound to RseA the latter is susceptible to DegS degradation.
CC Thus if periplasmic LPS levels increase the sigma-E regulon is induced
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with RseA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Partially
CC associates with the inner membrane via RseA. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Slight increase in basal sigma-E activity,
CC retains acid stress induction of sigma-E.
CC {ECO:0000269|PubMed:19170886}.
CC -!- SIMILARITY: Belongs to the RseB family. {ECO:0000305}.
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DR EMBL; CP001363; ACY89661.1; -; Genomic_DNA.
DR RefSeq; WP_000812017.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZSY7; -.
DR SMR; D0ZSY7; -.
DR EnsemblBacteria; ACY89661; ACY89661; STM14_3232.
DR KEGG; seo:STM14_3232; -.
DR PATRIC; fig|588858.6.peg.2999; -.
DR HOGENOM; CLU_054710_1_0_6; -.
DR OMA; DDFRYQY; -.
DR BioCyc; SENT588858:STM14_RS14445-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd16327; RseB; 1.
DR Gene3D; 3.30.200.100; -; 1.
DR InterPro; IPR033436; MucB/RseB_C.
DR InterPro; IPR038484; MucB/RseB_C_sf.
DR InterPro; IPR033434; MucB/RseB_N.
DR InterPro; IPR005588; MucB_RseB.
DR PANTHER; PTHR38782; PTHR38782; 1.
DR Pfam; PF03888; MucB_RseB; 1.
DR Pfam; PF17188; MucB_RseB_C; 1.
DR PIRSF; PIRSF005427; RseB; 1.
PE 3: Inferred from homology;
KW Periplasm; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..318
FT /note="Sigma-E factor regulatory protein RseB"
FT /id="PRO_0000424885"
SQ SEQUENCE 318 AA; 35768 MW; 684C9D7E351498DE CRC64;
MKQLWFAMSL VAASLFFSAN ASADPASGAL LQQMNIASQS LNYELSFVSI TKQGVESLRY
RHARLDGRPL AQLLQLDGPR REVVQRGNEI SYFEPGLEPF TLNGDYIVDS LPSLIYTDFK
RLAPYYDFIS VGRTRIADRL CEVIRVVARD GTRYSYIVWM DMDTKLPMRV DLLDRDGETL
EQFRVIAFTV SQDIGSNMQA LAKANLPPLL SVPGGEKTKF NWSPSWVPQG FSEVSSSRRP
LPTMDNLPIE SRLYSDGLFS FSVNVNRATQ NSSDQMLRTG RRTVYSSVRD NAEITIVGEL
PPQTAKRIAD SIKFRAVQ
