SYS_STAA8
ID SYS_STAA8 Reviewed; 428 AA.
AC P95689; Q2G2P9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine--tRNA ligase;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=serS; OrderedLocusNames=SAOUHSC_00009;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9565680; DOI=10.1016/s0167-4781(98)00027-x;
RA Bausch N., Seignovert L., Beaulande M., Leberman R., Hartlein M.;
RT "Analysis and overexpression in Escherichia coli of a staphylococcal gene
RT encoding seryl-tRNA synthetase.";
RL Biochim. Biophys. Acta 1397:169-174(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC probably able to aminoacylate tRNA(Sec) with serine, to form the
CC misacylated tRNA L-seryl-tRNA(Sec), which will be further converted
CC into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:9565680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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DR EMBL; Y09924; CAA71057.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29200.1; -; Genomic_DNA.
DR RefSeq; WP_000884334.1; NZ_LS483365.1.
DR RefSeq; YP_498617.1; NC_007795.1.
DR PDB; 6R1N; X-ray; 2.03 A; A=1-428.
DR PDBsum; 6R1N; -.
DR AlphaFoldDB; P95689; -.
DR SMR; P95689; -.
DR STRING; 1280.SAXN108_0011; -.
DR BindingDB; P95689; -.
DR ChEMBL; CHEMBL4523945; -.
DR EnsemblBacteria; ABD29200; ABD29200; SAOUHSC_00009.
DR GeneID; 3919182; -.
DR KEGG; sao:SAOUHSC_00009; -.
DR PATRIC; fig|93061.5.peg.9; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_1_1_9; -.
DR OMA; SPCFRRE; -.
DR BRENDA; 6.1.1.11; 3352.
DR UniPathway; UPA00906; UER00895.
DR PRO; PR:P95689; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR43697; PTHR43697; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..428
FT /note="Serine--tRNA ligase"
FT /id="PRO_0000122123"
FT BINDING 231..233
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 262..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 349..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 27..65
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 71..101
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 169..187
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:6R1N"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6R1N"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:6R1N"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6R1N"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 295..312
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:6R1N"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:6R1N"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:6R1N"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:6R1N"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:6R1N"
SQ SEQUENCE 428 AA; 48640 MW; 1ECADD668C63E655 CRC64;
MLDIRLFRNE PDTVKSKIEL RGDDPKVVDE ILELDEQRRK LISATEEMKA RRNKVSEEIA
LKKRNKENAD DVIAEMRTLG DDIKEKDSQL NEIDNKMTGI LCRIPNLISD DVPQGESDED
NVEVKKWGTP REFSFEPKAH WDIVEELKMA DFDRAAKVSG ARFVYLTNEG AQLERALMNY
MITKHTTQHG YTEMMVPQLV NADTMYGTGQ LPKFEEDLFK VEKEGLYTIP TAEVPLTNFY
RNEIIQPGVL PEKFTGQSAC FRSEAGSAGR DTRGLIRLHQ FDKVEMVRFE QPEDSWNALE
EMTTNAEAIL EELGLPYRRV ILCTGDIGFS ASKTYDLEVW LPSYNDYKEI SSCSNCTDFQ
ARRANIRFKR DKAAKPELAH TLNGSGLAVG RTFAAIVENY QNEDGTVTIP EALVPFMGGK
TQISKPVK
