Reviewed, UniProtKB/Swiss-Prot Q4V2X4 (CHEB2_BURMA)

Names and origin

Protein names

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

Gene names

Name:	cheB2
Ordered Locus Names:	BMAA0221.1

Organism

Burkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]

Taxonomic identifier

13373 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	342 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 – 342	342	Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099		PRO_0000225444
Regions
	Domain	2 – 119	118	Response regulatory
	Domain	144 – 337	194	CheB-type methylesterase
Sites
	Active site	159	1	By similarity
	Active site	186	1	By similarity
	Active site	279	1	By similarity
Amino acid modifications
	Modified residue	53	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4V2X4-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: E7BA20EC1E01B7DB	FASTA	342	36,134
	10 20 30 40 50 60 MNIGIVNDLP LAVEALRRTI ALRPEHRVLW VATDGAQALD FCVAQPPDLV LMDLVMPRID 70 80 90 100 110 120 GVSATRSIME RSPCAILIVT ANVGANASYV YEAMGAGALD AVDTPTLEQG GSADPSQPLL 130 140 150 160 170 180 AKIDQIGRLL ATRMPLAAPA AAAPAPQGAL PPLVAIGASA GGPTALTALL RRLPDDFPAA 190 200 210 220 230 240 LVIVQHVDQA FAIGMAQWLD GYSPLPVRIA RQGSVPQAGE VLLAATNDHL HLTSRGVLAY 250 260 270 280 290 300 TRRPEETPYR PSVDVFFHSV VDHWKGEAIG VLLTGMGRDG ALGLKAMRTK GHYTIAQDEA 310 320 330 340 TSAVYGMPKA AAAIGAASAV LPLERIADQL ISLVQRNRQR WR

References

[1]

"Structural flexibility in the Burkholderia mallei genome." Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M. , Kolonay J.F., Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004) [PubMed: 15377793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23344.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000011 Genomic DNA. Translation: AAY59282.1.
RefSeq	YP_338317.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3704284.
GenomeReviews	Gene locus BMAA0221.1 in contig CP000011_GR.
KEGG	bma:BMAA0221.1.
TIGR	BMAA0221.1.
Phylogenomic databases
HOGENOM	Q4V2X4.
OMA	Q4V2X4. EAMGHGA.
Enzyme and pathway databases
BioCyc	BMAL243160:BMA_A0221.1-MON.
BRENDA	3.1.1.61. 260531.
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_BURMA

Accession

Primary (citable) accession number: Q4V2X4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 34 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)