ID   CHEB2_AZOBR    STANDARD;      PRT;   394 AA.
AC   Q8VL08;
DT   25-OCT-2004 (Rel. 45, Created)
DT   25-OCT-2004 (Rel. 45, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Chemotaxis response regulator protein-glutamate methylesterase group 2
DE   operon (EC 3.1.1.61).
GN   Name=cheB;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp7 / ATCC 29145;
RX   PubMed=11934495;
RA   Hauwaerts D., Alexandre G., Das S.K., Vanderleyden J., Zhulin I.B.;
RT   "A major chemotaxis gene cluster in Azospirillum brasilense and
RT   relationships between chemotaxis operons in alpha-proteobacteria.";
RL   FEMS Microbiol. Lett. 208:61-67(2002).
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: Cytoplasmic.
CC   -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of
CC       the C-terminal effector domain.
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.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AF450326; AAL47024.1; -.
DR   HSSP; P04042; 1CHD.
DR   HAMAP; MF_00099; -; 1.
DR   InterPro; IPR000673; CheB_methylest.
DR   InterPro; IPR001789; Response_reg.
DR   InterPro; IPR008248; RR_chemtxs_CheB.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   ProDom; PD005328; CheB_methylest; 1.
DR   ProDom; PD000039; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
KW   Chemotaxis; Hydrolase; Phosphorylation; Sensory transduction.
FT   DOMAIN       27    145       Response regulatory.
FT   DOMAIN      191    393       CheB-type methylesterase.
FT   ACT_SITE    211    211       By similarity.
FT   ACT_SITE    238    238       By similarity.
FT   ACT_SITE    335    335       By similarity.
FT   MOD_RES      78     78       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   394 AA;  40986 MW;  55FBCF8D432A02BD CRC64;
     MSDGFGRPPP PAPAGHPTGA AGGDPVRVMV VDDSAVIRGL LTRALEGDTE IRVVASVGDG
     QMAVNALQRN SLDVIVLDIE MPVMDGLTAI PKLLAVAPQV KIIMASTLTL RGADISMRCL
     SAGAADYIPK PTSTREIGGA DAFKRELVSK VKALGAAARR AGSRTRGELR PLNPVPAAFL
     KREPPPVTLR PAPAVGSVGQ VKPDVIAIGS STGGPQALFE VLAHLKTGVT QPILITQHMP
     ATFTTILAEH ITRQCGMNAQ EAKDGEPVVP GRCYIAPGDF HMLVTQRAGA NVISLTKDPP
     ENFCRPAVDP MMRSILRAFG GRKVLACILT GMGQDGLKGC TEVVNAGGTL IAQDEASSVV
     WGMPGAVAQA GICSAVLPLK EIGPYIRKFA SRAA
//