ID   CHEB1_METMA             Reviewed;         357 AA.
AC   Q8Q009;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon;
DE            EC=3.1.1.61;
GN   Name=cheB1; OrderedLocusNames=MM_0329;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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: Cytoplasm.
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.
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DR   EMBL; AE008384; AAM30025.1; -; Genomic_DNA.
DR   RefSeq; NP_632353.2; -.
DR   HSSP; P04042; 1CHD.
DR   GeneID; 1478671; -.
DR   GenomeReviews; AE008384_GR; MM_0329.
DR   KEGG; mma:MM_0329; -.
DR   NMPDR; fig|192952.1.peg.329; -.
DR   HOGENOM; Q8Q009; -.
DR   OMA; Q8Q009; ACSEDTC.
DR   BioCyc; MMAZ192952:MM0329-MON; -.
DR   BRENDA; 3.1.1.61; 261165.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:HAMAP.
DR   GO; GO:0000156; F:two-component response regulator activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:HAMAP.
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   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:HAMAP.
DR   HAMAP; MF_00099; -; 1.
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   Gene3D; G3DSA:3.40.50.180; Chemotax_RR_pGlu_Me-esterase; 1.
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.
PE   3: Inferred from homology;
KW   Chemotaxis; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein.
FT   CHAIN         1    357       Chemotaxis response regulator protein-
FT                                glutamate methylesterase of group 1
FT                                operon.
FT                                /FTId=PRO_0000158053.
FT   DOMAIN       10    127       Response regulatory.
FT   DOMAIN      159    353       CheB-type methylesterase.
FT   ACT_SITE    171    171       By similarity.
FT   ACT_SITE    198    198       By similarity.
FT   ACT_SITE    295    295       By similarity.
FT   MOD_RES      61     61       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   357 AA;  38425 MW;  16FD4AF0D4EDF6B9 CRC64;
     MNEFGDSMIR TLIVDDSAFM RMAIRSMLAS SPDIKIAGDA CNGKEAVDKS KSLHPDIIIM
     DVNMPVMDGL TAVKTIMSTD PVPIIMFSTL TVEGSKEALE ALQLGAIDFV PKSESHHDVN
     KIEKELVDKI RNIHSSNPSI LRLINMRKFK GEVVRGKWSC AGDFAVLIGS STGGPSSLEQ
     VIPRLPGDLP APVFVVQHMP EGNFCKQLAE RLNFLSELEI KEARNNEKVT AGVVYIAPGG
     YHMTVKKALG VTRIKLIKSQ PVHAVMPAVD VIAESMLDVY GKNIVAAILT GMGFDGAAGF
     KKIRDAGGST IACSEDTCVI FGMPKAAIAA GGIDTVKPIF EIPEEIVRMS EVKCNGK
//