ID CHEB_SHIBS Reviewed; 312 AA.
AC Q322K2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase;
DE EC=3.1.1.61;
GN Name=cheB; OrderedLocusNames=SBO_1117;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Involved in the modulation of the chemotaxis system;
CC catalyzes the demethylation of specific methylglutamate residues
CC introduced into the chemoreceptors (methyl-accepting chemotaxis
CC proteins) by CheR (By similarity).
CC -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O
CC = protein L-glutamate + methanol.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of
CC the C-terminal effector domain (By similarity).
CC -!- PTM: Phosphorylated by CheA. Phosphorylation suppresses the
CC inhibitory activity of the N-terminal domain (By similarity).
CC -!- SIMILARITY: Contains 1 cheB-type methylesterase domain.
CC -!- SIMILARITY: Contains 1 response regulatory domain.
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DR EMBL; CP000036; ABB65756.1; -; Genomic_DNA.
DR RefSeq; YP_407584.1; NC_007613.1.
DR ProteinModelPortal; Q322K2; -.
DR SMR; Q322K2; 1-310.
DR STRING; 300268.SBO_1117; -.
DR EnsemblBacteria; ABB65756; ABB65756; SBO_1117.
DR GeneID; 3779673; -.
DR KEGG; sbo:SBO_1117; -.
DR PATRIC; 18681075; VBIShiBoy33460_1476.
DR eggNOG; COG2201; -.
DR HOGENOM; HOG000151423; -.
DR KO; K03412; -.
DR OMA; EAPVNRH; -.
DR BioCyc; SBOY300268:GJFL-1114-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:HAMAP.
DR GO; GO:0006935; P:chemotaxis; IEA:HAMAP.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:GOC.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IEA:HAMAP.
DR Gene3D; 3.40.50.180; -; 2.
DR HAMAP; MF_00099; CheB_methylest; 1; -.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008248; Sig_transdc_resp-reg_CheB.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF01339; CheB_methylest; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52738; Chemotax_RR_pGlu_Me-esterase; 1.
DR SUPFAM; SSF52172; CheY_like; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Chemotaxis; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein.
FT CHAIN 1 312 Chemotaxis response regulator protein-
FT glutamate methylesterase.
FT /FTId=PRO_0000225485.
FT DOMAIN 5 122 Response regulatory.
FT DOMAIN 152 307 CheB-type methylesterase.
FT ACT_SITE 164 164 By similarity.
FT ACT_SITE 190 190 By similarity.
FT ACT_SITE 249 249 By similarity.
FT MOD_RES 56 56 4-aspartylphosphate (By similarity).
SQ SEQUENCE 312 AA; 33655 MW; 731CF4B6AB80F3D6 CRC64;
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP DVLTLDVEMP
RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG AIDFVTKPQL GIREGMLAYS
EMIAEKVRTA AKASLAAHKP LSAPTTLKAG PLLSSEKLIA IGASTGGTEA IRHVLQPLPL
SSPALLITQH MPPGFTRSFA DRLNKLCQIG VKEAEDGERV LPGHAYIAPG DRHMELARSG
ANYQIKIHDG PVGMLAMRQA GAWTLAQNEA SCVVFGMPRE AINMGGVCEV VDLSQVSQQM
LAKISAGQAI RI
//
