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P99178 (SYS_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine--tRNA ligase
EC=6.1.1.11
Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:serS
Ordered Locus Names:SA0009
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_00176

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_00176

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP-Rule 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. HAMAP-Rule MF_00176

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Serine--tRNA ligase HAMAP-Rule MF_00176
PRO_0000122120

Regions

Nucleotide binding262 – 2643ATP By similarity
Nucleotide binding349 – 3524ATP By similarity
Region231 – 2333Serine binding By similarity

Sites

Binding site2851Serine By similarity
Binding site3851Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
P99178 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 19CAAD63D966B600

FASTA42848,640
        10         20         30         40         50         60 
MLDIRLFRNE PDTVKSKIEL RGDDPKVVDE ILELDEQRRK LISATEEMKA RRNKVSEEIA 

        70         80         90        100        110        120 
LKKRNKENAD DVIAEMRTLG DDIKEKDSQL NEIDNKMTGI LCRIPNLISD DVPQGESDED 

       130        140        150        160        170        180 
NVEVKKWGTP REFSFEPKAH WDIVEELKMA DFDRAAKVSG ARFVYLTNEG AQLERALMNY 

       190        200        210        220        230        240 
MITKHTTQHG YTEMMVPQLV NADTMYGTGQ LPKFEEDLFK VEKEGLYTIP TAEVPLTNFY 

       250        260        270        280        290        300 
RNEIIQPGVL PEKFTGQSAC FRSEAGSAGR DTRGLIRLHQ FDKVEMVRFE QPEDSWNALE 

       310        320        330        340        350        360 
EMTTNAEAIL EELGLPYRRV ILCTGDIGFS ASKTYDIEVW LPSYNDYKEI SSCSNCTDFQ 

       370        380        390        400        410        420 
ARRANIRFKR DKAAKPELAH TLNGSGLAVG RTFAAIVENY QNEDGTVTIP EALVPFMGGK 


TQISKPVK

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000018 Genomic DNA. Translation: BAB41225.1.
PIRA89759.
RefSeqNP_373247.1. NC_002745.2.

3D structure databases

ProteinModelPortalP99178.
SMRP99178. Positions 1-426.
ModBaseSearch...

Protein-protein interaction databases

STRING158879.SA0009.

2D gel databases

SWISS-2DPAGEP99178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB41225; BAB41225; BAB41225.
GeneID1122780.
KEGGsau:SA0009.
PATRIC19572035. VBIStaAur116463_0009.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000035937.
KOK01875.
OMAEESWEWH.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-9-MONOMER.
UniPathwayUPA00906; UER00895.

Family and domain databases

Gene3D1.10.287.40. 1 hit.
HAMAPMF_00176. Ser_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERPTHR11778. PTHR11778. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_STAAN
AccessionPrimary (citable) accession number: P99178
Secondary accession number(s): Q99XG2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents