Q2L1D1 (CHEB2_BORA1) Reviewed, UniProtKB/Swiss-Prot

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:	BAV1679

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
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. HAMAP MF_00099
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. HAMAP MF_00099
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: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-glutamate methylesterase activity Inferred from electronic annotation. Source: EC 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 – 351	351	Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099		PRO_0000264263
Regions
	Domain	5 – 122	118	Response regulatory
	Domain	154 – 347	194	CheB-type methylesterase
Sites
	Active site	166	1	By similarity
	Active site	192	1	By similarity
	Active site	289	1	By similarity
Amino acid modifications
	Modified residue	56	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2L1D1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: B2C5668E200C4937	FASTA	351	37,674
	10 20 30 40 50 60 MKKIRVICVD DSALVRGLMT EIINSHPDME VVATAPDPLV ARELIKQHNP DVLTLDVEMP 70 80 90 100 110 120 RMDGLDFLEK LMRLRPMPVV MVSSLTERGG EITMRALELG AIDFVTKPRL GIRDGLLDYS 130 140 150 160 170 180 ELIADKIRAA SRARLRGPAP VAAAALPARL RSPLNSSEKL VILGASTGGT EAIREVLLPL 190 200 210 220 230 240 PPDSPAILIT QHMPAGFTRS FAQRLDTLCA VTVREATHGE RVLPGHVYLA PGGEQHMKLG 250 260 270 280 290 300 RSGANYVIEL EAGEPVNRHR PSVDVLFHSA AQAAGRNAIG VLLTGMGKDG AAGLLAMKRA 310 320 330 340 350 GAYTLAQDEA SCVVFGMPRE AILLGAADEV VPLPAMSERI LMRAGDRGHR V

References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 197N.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM167904 Genomic DNA. Translation: CAJ49287.1.
RefSeq	YP_786197.1. NC_010645.1.
3D structure databases
ProteinModelPortal	Q2L1D1.
SMR	Q2L1D1. Positions 1-343.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2L1D1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6266778.
GenomeReviews	Gene locus BAV1679 in contig AM167904_GR.
KEGG	bav:BAV1679.
NMPDR	fig|521.1.peg.1737.
PATRIC	21129540. VBIBorAvi43433_1691.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG705324.
OMA	FVTKPKL.
ProtClustDB	PRK00742.
Enzyme and pathway databases
BioCyc	ABAU360910:BAV1679-MONOMER.
Family and domain databases
HAMAP	MF_00099. CheB_methylest. [Tree]
InterPro	IPR011006. CheY-like_superfamily. 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.
KO	K03412.
Pfam	PF01339. CheB_methylest. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
PIRSF	PIRSF000876. RR_chemtxs_CheB. 1 hit.
SMART	SM00448. REC. 1 hit. [Graphical view]
SUPFAM	SSF52738. Chemotax_RR_pGlu_Me-esterase. 1 hit. SSF52172. CheY_like. 1 hit.
PROSITE	PS50122. CHEB. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHEB2_BORA1

Accession

Primary (citable) accession number: Q2L1D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 7, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program