Q8F6P9 (CHEB1_LEPIN) 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:	LA_1252

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)

Taxonomic identifier

189518 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	357 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 – 357	357	Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099		PRO_0000158002
Regions
	Domain	7 – 125	119	Response regulatory
	Domain	162 – 355	194	CheB-type methylesterase
Sites
	Active site	174	1	By similarity
	Active site	201	1	By similarity
	Active site	297	1	By similarity
Amino acid modifications
	Modified residue	58	1	4-aspartylphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8F6P9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: FE34A505FEC17E6B	FASTA	357	38,712
	10 20 30 40 50 60 MIPNPVRAVI IDDSLLVRNI ISDQIQKDSK IHVVATGKTG MDCIDLAQKM NPDVIILDVE 70 80 90 100 110 120 MPVMDGLTAL HELQKKKLGI PVIMLSVLTQ NGAEATFKAL EYGAIDFVPK PSSVFQFDPE 130 140 150 160 170 180 EIGNILKSKI LAYFESKIQI PSQNLLKKAP AYSKVPAGSH LKKSPIQAIC IGTSTGGPRA 190 200 210 220 230 240 LQEVFSRIPA DISLPILVVQ HMPAGFTKAF ATRLNDHAKI KVKEAEDGEP IEPNTGYVAP 250 260 270 280 290 300 GDAHLSIQSK GGRKWIALNR EAPVNGHRPS IEVLLDSAIE EYKSGIIGVI MTGMGKDGSA 310 320 330 340 350 AIVRVREIGG STIAQDEQTS VIYGMNRQAV EMGGVEYIEP VTEIINRIQI ILKERGI

References

[1]

"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing." Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P. Nature 422:888-893(2003) [PubMed: 12712204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 56601.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010300 Genomic DNA. Translation: AAN48451.1.
RefSeq	NP_711433.1. NC_004342.2.
3D structure databases
ProteinModelPortal	Q8F6P9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1150595.
GenomeReviews	Gene locus LA_1252 in contig AE010300_GR.
KEGG	lil:LA_1252.
PATRIC	22383357. VBILepInt91350_1253.
Phylogenomic databases
HOGENOM	HBG705324.
OMA	VPIFVVQ.
PhylomeDB	Q8F6P9.
ProtClustDB	CLSK573833.
Enzyme and pathway databases
BioCyc	LINT189518:LA1252-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_LEPIN

Accession

Primary (citable) accession number: Q8F6P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program