Q88EW5 (CHEB1_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	cheB1
Ordered Locus Names:	PP_4337

Organism

Pseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]

Taxonomic identifier

160488 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	370 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
Miscellaneous	P.putida strain KT2440 does not have a chemotaxis group 2 operon. 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 – 370	370	Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099		PRO_0000158011
Regions
	Domain	4 – 121	118	Response regulatory
	Domain	179 – 370	192	CheB-type methylesterase
Sites
	Active site	194	1	By similarity
	Active site	221	1	By similarity
	Active site	314	1	By similarity
Amino acid modifications
	Modified residue	55	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q88EW5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D2405CD1B0B2399C	FASTA	370	39,452
	10 20 30 40 50 60 MAVKVLVVDD SGFFRRRVSE ILSADPTIQV VGTATNGKEA IDQALALKPD VITMDYEMPM 70 80 90 100 110 120 MDGITAVRHI MQRCPTPVLM FSSLTHEGAR VTLDALDAGA VDYLPKNFED ISRNPDKVKQ 130 140 150 160 170 180 LLCEKVHTIS RSNRRIGSYA RTAPVAAPAP ASTFTSQAQT RPAAPARAAA PTPAASQSPA 190 200 210 220 230 240 PKRKPYKLVA IGTSTGGPVA LQRVLTQLPA NFPAPIVLIQ HMPAAFTKAF AERLDKLCRI 250 260 270 280 290 300 SVKEAEDGDM LRPGLALLAP GGKQMMIDGR GTVKILPGDE RLNYKPCVDI TFGSAAKSYG 310 320 330 340 350 360 DKVLSVVLTG MGADGREGAR LLKQGGSTVW AQDEASCVIY GMPMAIVKAN LADAVYSLDE 370 IGKHLVEACV

References

[1]

"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440." Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O. , Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M. Environ. Microbiol. 4:799-808(2002) [PubMed: 12534463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KT2440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015451 Genomic DNA. Translation: AAN69916.1.
RefSeq	NP_746452.1. NC_002947.3.
3D structure databases
ProteinModelPortal	Q88EW5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q88EW5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1046087.
GenomeReviews	Gene locus PP_4337 in contig AE015451_GR.
KEGG	ppu:PP_4337.
NMPDR	fig|160488.1.peg.4282.
PATRIC	19947336. VBIPsePut30601_4611.
TIGR	PP_4337.
Phylogenomic databases
eggNOG	NOG76823.
HOGENOM	HBG705324.
OMA	YQLVAIG.
PhylomeDB	Q88EW5.
ProtClustDB	PRK00742.
Enzyme and pathway databases
BioCyc	PPUT160488:PP_4337-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

CHEB1_PSEPK

Accession

Primary (citable) accession number: Q88EW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program