P04042 (CHEB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	cheB
Ordered Locus Names:	STM1917

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). The MCP methylation state of the cell is crucial for sensory responses and adaptations. 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 domain interferes with esterase activity and is not essential for catalysis. HAMAP MF_00099
Post-translational modification	Phosphorylated by CheA. Ref.4 Two forms were isolated, the intact protein and a proteolytic fragment (146-349) that is 15-fold more active than its precursor. HAMAP MF_00099
Disruption phenotype	Cells lacking this gene display a strong clockwise motor bias; in combination with a yhjH disruption cells switch to a counterclockwise bias. Ref.6
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	3D-structure Complete proteome Direct protein sequencing 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 – 349

349

Chemotaxis response regulator protein-glutamate methylesterase HAMAP MF_00099

PRO_0000158027

Regions

Domain

5 – 122

118

Response regulatory

Domain

152 – 344

193

CheB-type methylesterase

Sites

Active site

164

1

Active site

190

1

Active site

286

1

Amino acid modifications

Modified residue

56

1

4-aspartylphosphate HAMAP MF_00099

Secondary structure

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349

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

13 – 24

12

Beta strand

29 – 37

9

Helix

38 – 48

11

Beta strand

51 – 56

6

Beta strand

60 – 62

3

Helix

64 – 73

10

Beta strand

79 – 83

5

Helix

87 – 99

13

Beta strand

103 – 106

4

Beta strand

108 – 111

4

Helix

116 – 132

17

Helix

135 – 138

4

Beta strand

158 – 163

6

Helix

167 – 175

9

Beta strand

184 – 189

6

Helix

195 – 206

12

Beta strand

208 – 213

6

Beta strand

224 – 227

4

Beta strand

232 – 239

8

Beta strand

242 – 248

7

Beta strand

253 – 255

3

Helix

260 – 270

11

Helix

272 – 274

3

Beta strand

275 – 279

5

Beta strand

283 – 285

3

Helix

288 – 297

10

Beta strand

300 – 304

5

Helix

306 – 308

3

Helix

313 – 319

7

Turn

320 – 322

3

Beta strand

325 – 328

4

Helix

330 – 341

12

Beta strand

343 – 345

3

Sequences

	Sequence		Length	Mass (Da)
	P04042 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 79BAFC2D202F2F8B	FASTA	349	37,552
	10 20 30 40 50 60 MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP DVLTLDVEMP 70 80 90 100 110 120 RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG AIDFVTKPQL GIREGMLAYS 130 140 150 160 170 180 EMIAEKVRTA ARARIAAHKP MAAPTTLKAG PLLSSEKLIA IGASTGGTEA IRHVLQPLPL 190 200 210 220 230 240 SSPAVIITQH MPPGFTRSFA ERLNKLCQIS VKEAEDGERV LPGHAYIAPG DKHMELARSG 250 260 270 280 290 300 ANYQIKIHDG PPVNRHRPSV DVLFHSVAKH AGRNAVGVIL TGMGNDGAAG MLAMYQAGAW 310 320 330 340 TIAQNEASCV VFGMPREAIN MGGVSEVVDL SQVSQQMLAK ISAGQAIRI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple forms of the CheB methylesterase in bacterial chemosensing." Simms S.A., Keane M.G., Stock J. J. Biol. Chem. 260:10161-10168(1985) [PubMed: 2991277] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Active site of the enzyme which demethylates receptors during bacterial chemotaxis." Simms S.A., Cornman E.W., Mottonen J., Stock J. J. Biol. Chem. 262:29-31(1987) [PubMed: 3539934] [Abstract] Cited for: PROTEIN SEQUENCE OF 277-306.
[4]	"Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis." Hess J.F., Oosawa K., Kaplan N., Simon M.I. Cell 53:79-87(1988) [PubMed: 3280143] [Abstract] Cited for: PHOSPHORYLATION.
[5]	"Activation of methylesterase CheB: evidence of a dual role for the regulatory domain." Anand G.S., Goudreau P.N., Stock A.M. Biochemistry 37:14038-14047(1998) [PubMed: 9760239] [Abstract] Cited for: CHARACTERIZATION.
[6]	"The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism." Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M. Mol. Cell 38:128-139(2010) [PubMed: 20346719] [Abstract] Cited for: DISRUPTION PHENOTYPE. Strain: ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023.
[7]	"Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB." West A.H., Martinez-Hackert E., Stock A.M. J. Mol. Biol. 250:276-290(1995) [PubMed: 7608974] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 152-349.
[8]	"Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain." Djordjevic S., Goudreau P.N., Xu Q., Stock A.M., West A.H. Proc. Natl. Acad. Sci. U.S.A. 95:1381-1386(1998) [PubMed: 9465023] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE006468 Genomic DNA. Translation: AAL20833.1.

PIR

XYEBET. A00547.

RefSeq

NP_460874.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2O	X-ray	2.40	A/B	1-349	[»]
1CHD	X-ray	1.75	A	147-349	[»]

ProteinModelPortal

P04042.

SMR

P04042. Positions 1-347.

ModBase

Search...

Proteomic databases

PRIDE

P04042.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1253438.

GenomeReviews

Gene locus STM1917 in contig AE006468_GR.

KEGG

stm:STM1917.

PATRIC

32382389. VBISalEnt20916_2033.

Phylogenomic databases

HOGENOM

HBG705324.

OMA

FVTKPKL.

ProtClustDB

PRK00742.

Enzyme and pathway databases

BioCyc

STYP99287:STM1917-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

CHEB_SALTY

Accession

Primary (citable) accession number: P04042

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program