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RSEB_ECO57
ID   RSEB_ECO57              Reviewed;         318 AA.
AC   P0AFY0; P46186;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Sigma-E factor regulatory protein RseB;
DE   Flags: Precursor;
GN   Name=rseB; OrderedLocusNames=Z3853, ECs3437;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG57687.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36860.1; -; Genomic_DNA.
DR   PIR; C85903; C85903.
DR   PIR; E91058; E91058.
DR   RefSeq; NP_311464.1; NC_002695.1.
DR   RefSeq; WP_000812053.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFY0; -.
DR   SMR; P0AFY0; -.
DR   STRING; 155864.EDL933_3736; -.
DR   EnsemblBacteria; AAG57687; AAG57687; Z3853.
DR   EnsemblBacteria; BAB36860; BAB36860; ECs_3437.
DR   GeneID; 66673540; -.
DR   GeneID; 914893; -.
DR   KEGG; ece:Z3853; -.
DR   KEGG; ecs:ECs_3437; -.
DR   PATRIC; fig|386585.9.peg.3591; -.
DR   eggNOG; COG3026; Bacteria.
DR   HOGENOM; CLU_054710_1_0_6; -.
DR   OMA; DDFRYQY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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_0000045239"
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
 
 
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