P62637 (CHEB2_DESVH) Reviewed, UniProtKB/Swiss-Prot

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:	cheB2
Ordered Locus Names:	DVU_2078

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length	367 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 Reference 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 – 367	367	Chemotaxis response regulator protein-glutamate methylesterase of group 2 operon HAMAP MF_00099		PRO_0000157991
Regions
	Domain	3 – 120	118	Response regulatory
	Domain	175 – 367	193	CheB-type methylesterase
Sites
	Active site	187	1	By similarity
	Active site	214	1	By similarity
	Active site	310	1	By similarity
Amino acid modifications
	Modified residue	54	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62637 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: FE21D478861A22E2	FASTA	367	39,075
	10 20 30 40 50 60 MISVVVVDDS AFMRKALSTM LEKDPEIRVV ATARDGEEGL QVIRQHNPDV VTLDIEMPRM 70 80 90 100 110 120 DGLTTLRHIM MEMPRPVLMV SSLTTEGAEA TLKALELGAV DFIPKQLSKV SLDIVRIEND 130 140 150 160 170 180 LREKVKEVSK RRMLRTPRPV RPAPTASAPA QTAQVASAAP ATAPSRPAMP ATRASRPVRD 190 200 210 220 230 240 VVAIGVSTGG PPAVQKVLSQ LPADFPASIL IAQHMPAAFT GPFAKRLDGV CAISVKEAES 250 260 270 280 290 300 GEKLKPGTAY IAPGGKHLRV EQRVSHMEVV VTTDPADALY KPSANVLMES VGQSMGRRAL 310 320 330 340 350 360 GVILTGMGSD GMEGMKVLKQ KGGRSIAQSD ATCVVYGMPK AIVDAGLADE IVDIDDMAAA IMNGLYK

References

[1]

"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. , Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hildenborough / ATCC 29579 / NCIMB 8303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017285 Genomic DNA. Translation: AAS96551.1.
RefSeq	YP_011291.1. NC_002937.3.
3D structure databases
ProteinModelPortal	P62637.
ModBase	Search...
Protein-protein interaction databases
STRING	P62637.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2793455.
GenomeReviews	Gene locus DVU_2078 in contig AE017285_GR.
KEGG	dvu:DVU2078.
NMPDR	fig|882.1.peg.2066.
PATRIC	32063842. VBIDesVul119526_1892.
TIGR	DVU_2078.
Phylogenomic databases
eggNOG	COG2201.
HOGENOM	HBG705324.
OMA	VPIFVVQ.
PhylomeDB	P62637.
ProtClustDB	CLSK705569.
Enzyme and pathway databases
BioCyc	DVUL882:DVU_2078-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_DESVH

Accession

Primary (citable) accession number: P62637

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program