Q1IQS9 (CHEB2_KORVE) 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:	Acid345_1770

Organism

Koribacter versatilis (strain Ellin345)

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	363 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 – 363	363	Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099		PRO_0000264254
Regions
	Domain	7 – 124	118	Response regulatory
	Domain	160 – 357	198	CheB-type methylesterase
Sites
	Active site	176	1	By similarity
	Active site	203	1	By similarity
	Active site	299	1	By similarity
Amino acid modifications
	Modified residue	58	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IQS9 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: AF7B13C54B72C59A	FASTA	363	38,701
	10 20 30 40 50 60 MRTTPIRVLV VDDSALMRKM ITQMLQKDPA IEVIGTAMDG AFGLKKIEEL RPDVVTLDLE 70 80 90 100 110 120 MPNMDGMEML RHITKRGQTP VIVVSAHTTQ GARETFKALQ LGAFDFVAKP QEGSSLTLEN 130 140 150 160 170 180 VADEIIAKIK VAGAARKPRP QIATVDEALL RSARKPARPP VASRTTPSKI IAIGISTGGP 190 200 210 220 230 240 NALLFMLSQL PADFAGTILI VQHMPEGFTQ MFSNRLAESC AIEVKEAASG DLLLAGRALI 250 260 270 280 290 300 CPGNRHMRVR RMPMGDVVVL SDEPPVNGHR PSADVLFRSV AQEFGPKVVA LIMTGMGEDG 310 320 330 340 350 360 ADAIGAVKAA GGLAVAQDEG SSVVFGMPKV AIERGNVNRV VALDALPNLL MVQSAAQRVS SFD

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin345.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000360 Genomic DNA. Translation: ABF40771.1.
RefSeq	YP_590845.1. NC_008009.1.
3D structure databases
ProteinModelPortal	Q1IQS9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IQS9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4072830.
GenomeReviews	Gene locus Acid345_1770 in contig CP000360_GR.
KEGG	aba:Acid345_1770.
NMPDR	fig|204669.6.peg.1754.
PATRIC	31980476. VBICanKor57425_1883.
Phylogenomic databases
eggNOG	COG2201.
HOGENOM	HBG705324.
OMA	DIPARMM.
PhylomeDB	Q1IQS9.
Enzyme and pathway databases
BioCyc	ABAC204669:ACID345_1770-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_KORVE

Accession

Primary (citable) accession number: Q1IQS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program