A3D4F2 (A3D4F2_SHEB5) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Probable chemoreceptor glutamine deamidase CheD HAMAP-Rule MF_01440
EC=3.5.1.44 HAMAP-Rule MF_01440

Gene names

Name:	cheD HAMAP-Rule MF_01440
Ordered Locus Names:	Sbal_2116 EMBL ABN61615.1

Organism

Shewanella baltica (strain OS155 / ATCC BAA-1091) [Complete proteome] [HAMAP] EMBL ABN61615.1

Taxonomic identifier

325240 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella › Shewanella baltica

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis By similarity. HAMAP-Rule MF_01440
Catalytic activity	Protein L-glutamine + H2O = protein L-glutamate + NH3. HAMAP-Rule MF_01440
Sequence similarities	Belongs to the CheD family. HAMAP-Rule MF_01440

Ontologies

Keywords
Biological process	Chemotaxis HAMAP-Rule MF_01440
Molecular function	Hydrolase HAMAP-Rule MF_01440
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from electronic annotation. Source: HAMAP
Molecular_function	protein-glutamine glutaminase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A3D4F2 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 1D602CAFBBE6B581	FASTA	206	23,042
	10 20 30 40 50 60 MLKPNIEYAV TEPNRYHDSH FGCDAVKILP GEYFATRENT MIVTVLGSCV SVCLYDPKLK 70 80 90 100 110 120 IGGMNHFLLP SDNSNSTGVL ADSARYGVYA MELLLNDLLK LGARRSAIEA KVFGGGNMLQ 130 140 150 160 170 180 GFTLHNIGER NAEFVIEYLN TENIPIIAAD LLDVYPRKVY FFPHTGKVKV RKIKSLHNST 190 200 ILDRESEYRL RVRNLPTGGD VELFGD

References

[1]

"Complete sequence of chromosome of Shewanella baltica OS155." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OS155 / ATCC BAA-1091.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000563 Genomic DNA. Translation: ABN61615.1.
RefSeq	YP_001050484.1. NC_009052.1.
3D structure databases
ProteinModelPortal	A3D4F2.
ModBase	Search...
Protein-protein interaction databases
STRING	325240.Sbal_2116.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN61615; ABN61615; Sbal_2116.
GeneID	4842672.
KEGG	sbl:Sbal_2116.
PATRIC	37183169. VBISheBal55297_2422.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1871.
HOGENOM	HOG000273194.
KO	K03411.
OMA	HNIGERN.
ProtClustDB	PRK13487.
Family and domain databases
HAMAP	MF_01440. CheD.
InterPro	IPR005659. Chemorcpt_Glu_NH3ase_CheD. [Graphical view]
Pfam	PF03975. CheD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A3D4F2_SHEB5

Accession

Primary (citable) accession number: A3D4F2

Entry history

Integrated into UniProtKB/TrEMBL:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)