Q2KV65 (CHEB1_BORA1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chemotaxis response regulator protein-glutamate methylesterase 1
EC=3.1.1.61

Gene names

Name:	cheB1
Ordered Locus Names:	BAV1025

Organism

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

Taxonomic identifier

360910 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	342 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 – 342	342	Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099		PRO_0000264262
Regions
	Domain	2 – 119	118	Response regulatory
	Domain	146 – 336	191	CheB-type methylesterase
Sites
	Active site	158	1	By similarity
	Active site	185	1	By similarity
	Active site	278	1	By similarity
Amino acid modifications
	Modified residue	53	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2KV65 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 6981B5D7A5B8AD50	FASTA	342	36,012
	10 20 30 40 50 60 MRVAIVNDMP LAVEALRRSL AHDPELSLAW IASDGLQAVR RCAADLPDVI LMDLMMPVMN 70 80 90 100 110 120 GVEATRLIMA ESPCAIIVVT SDVLQHTSLV FEAMGHGALD AVDTPVLGRG DPKAAAQRLL 130 140 150 160 170 180 RKIRNAGWLI GKKTVALERT TAMASSDTDA ALVVIGASAG GPPSLAAVLR ALPASFPAAI 190 200 210 220 230 240 VLVQHVDAAF TSGMAAWLNE QCVLPVRLAS DGLRPEAGVV LLAGAGEHLV LGAERKLHYT 250 260 270 280 290 300 TEPRESVYSP SIDVFFHSVA QHWRGRAAGV LLTGMGQDGA LGLKAMRERG FFTIAQDRAT 310 320 330 340 SAVYGMPKAA AALDAACEIL PLGDIAPRLE KVFAPPANPL FN

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: CAJ48634.1.
RefSeq	YP_785548.1. NC_010645.1.
3D structure databases
ProteinModelPortal	Q2KV65.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2KV65.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6266771.
GenomeReviews	Gene locus BAV1025 in contig AM167904_GR.
KEGG	bav:BAV1025.
NMPDR	fig|521.1.peg.702.
PATRIC	21128254. VBIBorAvi43433_1051.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG705324.
OMA	KIGIVND.
ProtClustDB	PRK12555.
Enzyme and pathway databases
BioCyc	ABAU360910:BAV1025-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	K13491.
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

CHEB1_BORA1

Accession

Primary (citable) accession number: Q2KV65

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 7, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program