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SYS_MICLC
ID   SYS_MICLC               Reviewed;         427 AA.
AC   C5C878;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Mlut_01150;
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS   NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=465515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC   2665 / VKM Ac-2230;
RX   PubMed=19948807; DOI=10.1128/jb.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA   Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA   Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA   Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
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; CP001628; ACS29680.1; -; Genomic_DNA.
DR   RefSeq; WP_010079681.1; NZ_WBMF01000023.1.
DR   AlphaFoldDB; C5C878; -.
DR   SMR; C5C878; -.
DR   STRING; 465515.Mlut_01150; -.
DR   PRIDE; C5C878; -.
DR   EnsemblBacteria; ACS29680; ACS29680; Mlut_01150.
DR   KEGG; mlu:Mlut_01150; -.
DR   PATRIC; fig|465515.4.peg.93; -.
DR   eggNOG; COG0172; Bacteria.
DR   HOGENOM; CLU_023797_0_1_11; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; 353391at2; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000000738; 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; PTHR11778; PTHR11778; 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..427
FT                   /note="Serine--tRNA ligase"
FT                   /id="PRO_1000203763"
FT   BINDING         230..232
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         260..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         283
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         347..350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         387
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   427 AA;  46755 MW;  12348DA11E6383D5 CRC64;
     MIDVKDLIEQ PEKYRASQEA RGEDASLVDR VVEADAARRS SIAGFEQLRA EQKAFGKRVA
     QAKGEEKQAL LAEVKDLAAR VKEAESAAGA AEARLAELQR AFPNLIVDGV PAGGEDDFVV
     LKEVGTPRDF AAEGFEPRDH LELGELLGAI DMERGAKVSG ARFSFLTGVG ARLELALMQL
     GLDLALENGF VPVIPPTLVR PETMQGTGFD VEHDDEIYRL ERDDLYLVGT SEVALAGFHA
     GEIMDVSAPV RYAGWSTCYR REAGSAGKDT RGIIRVHQFN KLEMFIYAAQ EDAEAEHARL
     LAWEERMLGA IEVPYRVIDI AAGDLGLSAA RKFDCEAWVP TQGTYRELTS TSNCTTFQAR
     RLNIRERVRT EDGSKGGTRM VATLNGTLAT TRWIVAILEN HQNADGSVTV PAALRPYLGG
     MERFELV
 
 
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