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SYS_LACLA
ID   SYS_LACLA               Reviewed;         423 AA.
AC   Q9CEX2;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; OrderedLocusNames=LL1712;
GN   ORFNames=L150515;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is involved in tRNA binding.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00176}.
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DR   EMBL; AE005176; AAK05810.1; -; Genomic_DNA.
DR   PIR; H86838; H86838.
DR   RefSeq; NP_267868.1; NC_002662.1.
DR   RefSeq; WP_003130891.1; NC_002662.1.
DR   AlphaFoldDB; Q9CEX2; -.
DR   SMR; Q9CEX2; -.
DR   STRING; 272623.L150515; -.
DR   PaxDb; Q9CEX2; -.
DR   EnsemblBacteria; AAK05810; AAK05810; L150515.
DR   GeneID; 60356405; -.
DR   KEGG; lla:L150515; -.
DR   PATRIC; fig|272623.7.peg.1836; -.
DR   eggNOG; COG0172; Bacteria.
DR   HOGENOM; CLU_023797_1_1_9; -.
DR   OMA; SPCFRRE; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000002196; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..423
FT                   /note="Serine--tRNA ligase"
FT                   /id="PRO_0000122064"
FT   BINDING         231..233
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         262..264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         285
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         349..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         384
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   423 AA;  47469 MW;  6E21E5B3240B0FD9 CRC64;
     MLDIKKIRAD FDGVAAKLAT RGVEKEKLEK LHDLDIKRRE LIVKSEALKA ERNSVSDEIS
     QVKRAKGDAS AQIAAMQKVS AEIKAIDAEL AEIEENLNEI IIMLPNLPHE STPIGADEDD
     NVEVRRVGQT PTFNFEPKAH WDLGEDLGIL DWERGGKVTG SRFLFYKGAG ARLERALYNF
     MLDEHGKEGY TEMITPYMVN QESMFGTGQY PKFKEDTFEL KDDRGFVLIP TAEVPLTNYY
     RGEILDGAEL PIKFTAMSPS FRSEAGSAGR DTRGLIRLHQ FHKVEMVKFA KPDQSYDELE
     KMTANAENIL QKLGLAYRVV ALSTGDMGFS AAKTYDLEVW IPAQNTYREI SSCSNCEDFQ
     ARRAQIRYRD EEGKVQLLHT LNGSGLAVGR TVAAILENYQ NEDGSITVPE VLRPYMGGLE
     VIK
 
 
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