RSEB_HAEIN
ID RSEB_HAEIN Reviewed; 315 AA.
AC P44792;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sigma-E factor regulatory protein RseB;
DE Flags: Precursor;
GN Name=rseB; OrderedLocusNames=HI_0630;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22290.1; -; Genomic_DNA.
DR PIR; H64082; H64082.
DR RefSeq; NP_438790.1; NC_000907.1.
DR RefSeq; WP_005694646.1; NC_000907.1.
DR AlphaFoldDB; P44792; -.
DR SMR; P44792; -.
DR STRING; 71421.HI_0630; -.
DR DNASU; 949706; -.
DR EnsemblBacteria; AAC22290; AAC22290; HI_0630.
DR KEGG; hin:HI_0630; -.
DR PATRIC; fig|71421.8.peg.656; -.
DR eggNOG; COG3026; Bacteria.
DR HOGENOM; CLU_054710_1_0_6; -.
DR OMA; DDFRYQY; -.
DR PhylomeDB; P44792; -.
DR BioCyc; HINF71421:G1GJ1-657-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0045152; F:antisigma factor binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0032885; P:regulation of polysaccharide biosynthetic process; IBA:GO_Central.
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..315
FT /note="Sigma-E factor regulatory protein RseB"
FT /id="PRO_0000022250"
SQ SEQUENCE 315 AA; 35907 MW; 4FA6BC3FA76EB5CA CRC64;
MKKIPLKFTA LSLSLLLSSI ASAEELSAKQ SLDKMTQALD NLNYEIAFVQ TTPANMDSFR
YRHIKQDNKT YAQLVTLDGR QQEIIQRDNL VSYFQPNAQA FTLNSGNIVD AMPAVVRANF
DKLSSDYDFV KLGKDRVAGR FADTIRIVPK DDFRYQYLVF IDEENGLLLR SDMLDREGKL
LDQFRVVTLY IDDRLRGLTD YINKVSLPPL LKESKNEQSS DITWSAGWLP QGFSLIRYTQ
EILENEIIDS ALYSDGLFTF TLFVSNVGSN DLPENTWKQG AYTIYSEVIG GKEITFIGQL
PISTAKRIVQ EVKFR