Reviewed, UniProtKB/Swiss-Prot Q8PX96 (CHEB2_METMA)

Names and origin

Protein names

Recommended name:
    Chemotaxis response regulator protein-glutamate methylesterase of group 2 operon
    EC=3.1.1.61

Gene names

Name:	cheB
Ordered Locus Names:	MM_1326

Organism

Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]

Taxonomic identifier

2209 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by cheR By similarity.
Catalytic activity	Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol. HAMAP MF_00099
Subcellular location	Cytoplasm. HAMAP MF_00099
Domain	The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain. HAMAP MF_00099
Post-translational modification	Phosphorylated by cheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain By similarity.
Sequence similarities	Contains 1 cheB-type methylesterase domain. Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	Chemotaxis
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chemotaxis Inferred from electronic annotation. Source: HAMAP regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro sensory perception of chemical stimulus Inferred from electronic annotation. Source: HAMAP two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-glutamate methylesterase activity Inferred from electronic annotation. Source: HAMAP two-component response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 367	367	Chemotaxis response regulator protein-glutamate methylesterase of group 2 operon HAMAP MF_00099		PRO_0000158054
Regions
	Domain	15 – 132	118	Response regulatory
	Domain	172 – 367	196	CheB-type methylesterase
Sites
	Active site	184	1	By similarity
	Active site	211	1	By similarity
	Active site	311	1	By similarity
Amino acid modifications
	Modified residue	66	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PX96-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: A7C706F4DD55695A	FASTA	367	39,888
	10 20 30 40 50 60 MSNQHPKKVL EMVIRALIVD DSALIRKVLS DILNQDPKIA VIGTAINGED GLEKVRKLKP 70 80 90 100 110 120 DVVLLDNIMP VLDGLKTLSH IMEEFPTPVV IVSALGEKAE EITLTALEYG AVDVIEKPSG 130 140 150 160 170 180 ILSQSMHEMA EEICAKVRAV SKADLNNLGC IRDLEHQIPE NHRKKKNSLR EKTSVRNVLA 190 200 210 220 230 240 IGASTGGPRA LEKLIGSFPA EIPAAVLIVQ HMPPGFTASL SKRLDAKSAL RVKEAQEGDI 250 260 270 280 290 300 MEEGTVFIAP GDYHMEIVRN KVNGFGEDTV HLSCGPKELG SRPSVNVLFR SVARIYGPRV 310 320 330 340 350 360 ISLVLTGMNC DGADGAEEIK KMGGKVIAED QSSCVIYGMP GEIVRRNLAD FVLPLDKMAD EIVKIVR

References

[1]

"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G. J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008384 Genomic DNA. Translation: AAM31022.1.
RefSeq	NP_633350.1.
3D structure databases
HSSP	HSSP built from PDB template 1TMY based on UniProtKB Q56312.
ModBase	Search...
Genome annotation databases
GeneID	1479668.
GenomeReviews	Gene locus MM_1326 in contig AE008384_GR.
KEGG	mma:MM_1326.
NMPDR	fig|192952.1.peg.1326.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8PX96.
OMA	NCDGADG.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM1326-MON.
BRENDA	3.1.1.61. 261165.
Family and domain databases
HAMAP	MF_00099. [Tree]
InterPro	IPR008248. Sig_transdc_resp-reg_CheB. IPR000673. Sig_transdc_resp-reg_Me-estase. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Gene3D	G3DSA:3.40.50.180. Chemotax_RR_pGlu_Me-esterase. 1 hit.
Pfam	PF01339. CheB_methylest. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
PIRSF	PIRSF000876. RR_chemtxs_CheB. 1 hit.
ProDom	PD005328. CheB_methylest. 1 hit. PD000039. Response_reg. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00448. REC. 1 hit. [Graphical view]
PROSITE	PS50122. CHEB. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHEB2_METMA

Accession

Primary (citable) accession number: Q8PX96

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	October 1, 2002
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)