Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chemoreceptor glutamine deamidase CheD

Gene

cheD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA. In addition, deamidates other chemoreceptors, including McpB and McpC. CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. CheD is absolutely required for a behavioral response mediated by McpC but is not required for the response to asparagine mediated by McpB. CheD is necessary for the generation of wild-type prestimulus CheA autophosphorylation levels. Also required for methylation of MCPs by CheR. In addition, enhances the activity of CheC 5-fold in vitro.3 Publications

Catalytic activityi

Protein L-glutamine + H2O = protein L-glutamate + NH3.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciBSUB:BSU16460-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemoreceptor glutamine deamidase CheD (EC:3.5.1.44)
Gene namesi
Name:cheD
Synonyms:ylxK
Ordered Locus Names:BSU16460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells exhibit poorly methylated receptors, are tumbly and have a decreased sensitivity to attractants.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 166166Chemoreceptor glutamine deamidase CheDPRO_0000089639Add
BLAST

Proteomic databases

PaxDbiP40404.

Interactioni

Subunit structurei

Forms a complex with CheC.

Protein-protein interaction databases

IntActiP40404. 3 interactions.
STRINGi224308.Bsubs1_010100009076.

Structurei

3D structure databases

ProteinModelPortaliP40404.
SMRiP40404. Positions 6-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CheD family.Curated

Phylogenomic databases

eggNOGiCOG1871. LUCA.
HOGENOMiHOG000273195.
InParanoidiP40404.
KOiK03411.
OMAiNNGRRIM.
OrthoDBiEOG6WHNQB.
PhylomeDBiP40404.

Family and domain databases

HAMAPiMF_01440. CheD.
InterProiIPR005659. Chemorcpt_Glu_NH3ase_CheD.
IPR011324. Cytotoxic_necrot_fac-like_cat.
[Graphical view]
PfamiPF03975. CheD. 1 hit.
[Graphical view]
SUPFAMiSSF64438. SSF64438. 1 hit.

Sequencei

Sequence statusi: Complete.

P40404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTEAVVIK VGIADVKIAR FPDTIRTSGL GSCVGLVLYD KEKQTAGLVH
60 70 80 90 100
VMLPDSTLSK TAELNRAKYA DTAVQTTIDM LIEAGCRKFA LKAKLAGGSE
110 120 130 140 150
MFKFKSTNDL MKIGPRNVLA IKEQLSLFNI PIISEDTGGS SGRTIEFEPK
160
SCMLHIRTVK QGEKTI
Length:166
Mass (Da):18,008
Last modified:February 1, 1995 - v1
Checksum:i3932F57E08C29ED8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20144 Genomic DNA. Translation: AAA61469.1.
AL009126 Genomic DNA. Translation: CAB13519.1.
PIRiB55216.
RefSeqiNP_389528.1. NC_000964.3.
WP_003244852.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13519; CAB13519; BSU16460.
GeneIDi939959.
KEGGibsu:BSU16460.
PATRICi18975099. VBIBacSub10457_1741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20144 Genomic DNA. Translation: AAA61469.1.
AL009126 Genomic DNA. Translation: CAB13519.1.
PIRiB55216.
RefSeqiNP_389528.1. NC_000964.3.
WP_003244852.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP40404.
SMRiP40404. Positions 6-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP40404. 3 interactions.
STRINGi224308.Bsubs1_010100009076.

Proteomic databases

PaxDbiP40404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13519; CAB13519; BSU16460.
GeneIDi939959.
KEGGibsu:BSU16460.
PATRICi18975099. VBIBacSub10457_1741.

Phylogenomic databases

eggNOGiCOG1871. LUCA.
HOGENOMiHOG000273195.
InParanoidiP40404.
KOiK03411.
OMAiNNGRRIM.
OrthoDBiEOG6WHNQB.
PhylomeDBiP40404.

Enzyme and pathway databases

BioCyciBSUB:BSU16460-MONOMER.

Family and domain databases

HAMAPiMF_01440. CheD.
InterProiIPR005659. Chemorcpt_Glu_NH3ase_CheD.
IPR011324. Cytotoxic_necrot_fac-like_cat.
[Graphical view]
PfamiPF03975. CheD. 1 hit.
[Graphical view]
SUPFAMiSSF64438. SSF64438. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, and disruption of the Bacillus subtilis sigma 28 gene."
    Helmann J.D., Marquez L.M., Chamberlin M.J.
    J. Bacteriol. 170:1568-1574(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Chemotactic methylation and behavior in Bacillus subtilis: role of two unique proteins, CheC and CheD."
    Rosario M.M.L., Kirby J.R., Bochar D.A., Ordal G.W.
    Biochemistry 34:3823-3831(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN CHEMOTAXIS, DISRUPTION PHENOTYPE.
  4. "CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins."
    Rosario M.M.L., Ordal G.W.
    Mol. Microbiol. 21:511-518(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHEC.
  5. "Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis."
    Kristich C.J., Ordal G.W.
    J. Biol. Chem. 277:25356-25362(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEAMIDATION OF MCPA; MCPB AND MCPC.
  6. "Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade."
    Szurmant H., Muff T.J., Ordal G.W.
    J. Biol. Chem. 279:21787-21792(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF CHEC.

Entry informationi

Entry nameiCHED_BACSU
AccessioniPrimary (citable) accession number: P40404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 17, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.