RSEB_SHIFL
ID RSEB_SHIFL Reviewed; 318 AA.
AC P0AFY1; P46186;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Sigma-E factor regulatory protein RseB;
DE Flags: Precursor;
GN Name=rseB; OrderedLocusNames=SF2633, S2806;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- SIMILARITY: Belongs to the RseB family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44130.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17954.1; -; Genomic_DNA.
DR RefSeq; NP_708423.1; NC_004337.2.
DR RefSeq; WP_000812053.1; NZ_WPGW01000044.1.
DR AlphaFoldDB; P0AFY1; -.
DR SMR; P0AFY1; -.
DR STRING; 198214.SF2633; -.
DR EnsemblBacteria; AAN44130; AAN44130; SF2633.
DR EnsemblBacteria; AAP17954; AAP17954; S2806.
DR GeneID; 1027220; -.
DR GeneID; 66673540; -.
DR KEGG; sfl:SF2633; -.
DR KEGG; sfx:S2806; -.
DR PATRIC; fig|198214.7.peg.3141; -.
DR HOGENOM; CLU_054710_1_0_6; -.
DR OMA; DDFRYQY; -.
DR OrthoDB; 1490766at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 Lipid-binding; Periplasm; Reference proteome; Signal; Transcription;
KW Transcription regulation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..318
FT /note="Sigma-E factor regulatory protein RseB"
FT /id="PRO_0000045240"
SQ SEQUENCE 318 AA; 35750 MW; 3F8C34DD85600B54 CRC64;
MKQLWFAMSL VTGSLLFSAN ASATPASGAL LQQMNLASQS LNYELSFISI NKQGVESLRY
RHARLDNRPL AQLLQMDGPR REVVQRGNEI SYFEPGLEPF TLNGDYIVDS LPSLIYTDFK
RLSPYYDFIS VGRTRIADRL CEVIRVVARD GTRYSYIVWM DTESKLPMRV DLLDRDGETL
EQFRVIAFNV NQDISSSMQT LAKANLPPLL SVPVGEKAKF SWTPTWLPQG FSEVSSSRRP
LPTMDNMPIE SRLYSDGLFS FSVNVNRATP SSTDQMLRTG RRTVSTSVRD NAEITIVGEL
PPQTAKRIAE NIKFGAAQ