Reviewed, UniProtKB/Swiss-Prot P0A8L1 (SYS_ECOLI)

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:	b0893, JW0876

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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). Ref.6 Ref.9 Ref.10
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. Ref.10 Ref.8
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. Ref.9 Ref.8
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=64 µM for serine Ref.9 Ref.10 KM=0.068 µM for ATP

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 Ref.10 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Ref.10 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 430	430	Seryl-tRNA synthetase HAMAP MF_00176		PRO_0000122044
Regions
	Nucleotide binding	268 – 270	3	ATP By similarity
	Nucleotide binding	355 – 358	4	ATP By similarity
	Region	237 – 239	3	Serine binding By similarity
Sites
	Binding site	291	1	Serine By similarity
	Binding site	391	1	Serine By similarity
Experimental info
	Mutagenesis	355	1	E → Q: Loss of serine activation activity. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P0A8L1-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 87675745A512A626	FASTA	430	48,414
	10 20 30 40 50 60 MLDPNLLRNE PDAVAEKLAR RGFKLDVDKL GALEERRKVL QVKTENLQAE RNSRSKSIGQ 70 80 90 100 110 120 AKARGEDIEP LRLEVNKLGE ELDAAKAELD ALQAEIRDIA LTIPNLPADE VPVGKDENDN 130 140 150 160 170 180 VEVSRWGTPR EFDFEVRDHV TLGEMHSGLD FAAAVKLTGS RFVVMKGQIA RMHRALSQFM 190 200 210 220 230 240 LDLHTEQHGY SENYVPYLVN QDTLYGTGQL PKFAGDLFHT RPLEEEADTS NYALIPTAEV 250 260 270 280 290 300 PLTNLVRGEI IDEDDLPIKM TAHTPCFRSE AGSYGRDTRG LIRMHQFDKV EMVQIVRPED 310 320 330 340 350 360 SMAALEEMTG HAEKVLQLLG LPYRKIILCT GDMGFGACKT YDLEVWIPAQ NTYREISSCS 370 380 390 400 410 420 NVWDFQARRM QARCRSKSDK KTRLVHTLNG SGLAVGRTLV AVMENYQQAD GRIEVPEVLR 430 PYMNGLEYIG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the gene for Escherichia coli seryl-tRNA synthetase." Haertlein M., Madern D., Leberman R. Nucleic Acids Res. 15:1005-1017(1987) [PubMed: 3029694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H. Mol. Microbiol. 2:785-795(1988) [PubMed: 3062312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-430.
[6]	"Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine." Leinfelder W., Zehelein E., Mandrand-Berthelot M.A., Boeck A. Nature 331:723-725(1988) [PubMed: 2963963] [Abstract] Cited for: FUNCTION AS A SERYL-TRNA(SEC) SYNTHETASE.
[7]	"Escherichia coli seryl-tRNA synthetase: the structure of a class 2 aminoacyl-tRNA synthetase." Leberman R., Haertlein M., Cusack S. Biochim. Biophys. Acta 1089:287-298(1991) [PubMed: 1859832] [Abstract] Cited for: REVIEW.
[8]	"Crystallization of the seryl-tRNA synthetase:tRNA(Ser) complex of Escherichia coli." Price S., Cusack S., Borel F., Berthet-Colominas C., Leberman R. FEBS Lett. 324:167-170(1993) [PubMed: 8508916] [Abstract] Cited for: SUBUNIT, DOMAIN, CRYSTALLIZATION.
[9]	"Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity." Borel F., Vincent C., Leberman R., Haertlein M. Nucleic Acids Res. 22:2963-2969(1994) [PubMed: 8065908] [Abstract] Cited for: FUNCTION, KINETIC PARAMETERS, DOMAIN.
[10]	"Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation." Vincent C., Borel F., Willison J.C., Leberman R., Haertlein M. Nucleic Acids Res. 23:1113-1118(1995) [PubMed: 7537870] [Abstract] Cited for: FUNCTION, KINETIC PARAMETERS, MUTAGENESIS OF GLU-355, SUBUNIT, REACTION MECHANISM.
[11]	"A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A." Cusack S., Berthet-Colominas C., Haertlein M., Nassar N., Leberman R. Nature 347:249-255(1990) [PubMed: 2205803] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases
EMBLGenBankDDBJ	X05017 Genomic DNA. Translation: CAA28673.1. U00096 Genomic DNA. Translation: AAC73979.1. AP009048 Genomic DNA. Translation: BAA35625.1. J03412 Genomic DNA. Translation: AAA83842.1.
PIR	YSEC. A26400.
RefSeq	AP_001523.1. NP_415413.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A8L1. 16 interactions.
STRING	P0A8L1.
2-D gel databases
SWISS-2DPAGE	P0A8L1.
2DBase-Ecoli	P0A8L1.
ECO2DBASE	E048.8. 6TH EDITION.
Genome annotation databases
GeneID	945506.
GenomeReviews	Gene locus JW0876 in contig AP009048_GR. Gene locus b0893 in contig U00096_GR.
KEGG	ecj:JW0876. eco:b0893.
Organism-specific databases
EchoBASE	EB0940.
EcoGene	EG10947. serS.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG629391.
OMA	AHWDLGP.
Enzyme and pathway databases
BioCyc	EcoCyc:SERS-MON. ECOL168927:B0893-MON. MetaCyc:SERS-MON.
Gene expression databases
Genevestigator	P0A8L1.
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. IPR010978. tRNA_bd_arm. [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.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_ECOLI

Accession

Primary (citable) accession number: P0A8L1
Secondary accession number(s): P09156

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	December 15, 2009
This is version 46 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)