Reviewed, UniProtKB/Swiss-Prot A7GJT0 (SYS_BACCN)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS

Gene names

Name:	serS
Ordered Locus Names:	Bcer98_0012

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 424	424	Seryl-tRNA synthetase HAMAP MF_00176		PRO_1000077185
Regions
	Nucleotide binding	262 – 264	3	ATP By similarity
	Nucleotide binding	349 – 352	4	ATP By similarity
	Region	231 – 233	3	Serine binding By similarity
Sites
	Binding site	285	1	Serine By similarity
	Binding site	385	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GJT0-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: B41AAA8314E26948	FASTA	424	48,769
	10 20 30 40 50 60 MLDIKFLRAN FEEVKEKLQH RGEDLADFEC FEELDTKRRE LLVQTEELKS KRNEVSQQIS 70 80 90 100 110 120 MLKREKKDAE ALILEMREVG EKIKGLDNEL REVEEDLERL MLSIPNIPHE STPVGETEDD 130 140 150 160 170 180 NVVVRTWGEV KEFNFEPKPH WDLATDLGIV DFERAGKVTG SRFVFYKGAG ARLERALISF 190 200 210 220 230 240 MLDLHTEEHG YEEVLPPYMV NRASMTGTGQ LPKFEEDAFL IESEDYFLIP TAEVPVTNMH 250 260 270 280 290 300 RDEILSAEQL PIRYAAFSSC FRSEAGSAGR DTRGLIRQHQ FNKVELVKFV KPEESYEELE 310 320 330 340 350 360 KLTNDAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW LPSYDTYREI SSCSNFEAFQ 370 380 390 400 410 420 ARRANIRFRR EPNAKPEPVH TLNGSGLAIG RTVAAILENY QQEDGTIIIP EVLRPYMGGK TVIK

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000764 Genomic DNA. Translation: ABS20388.1.
RefSeq	YP_001373383.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7GJT0.
Genome annotation databases
GeneID	5344991.
GenomeReviews	Gene locus Bcer98_0012 in contig CP000764_GR.
KEGG	bcy:Bcer98_0012.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	LKPYMGG.
Family and domain databases
HAMAP	MF_00176. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTS	PR00981. TRNASYNTHSER.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_BACCN

Accession

Primary (citable) accession number: A7GJT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)