SYK_MYCFP
ID SYK_MYCFP Reviewed; 488 AA.
AC Q49158; C4XFK3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=MBIO_0660;
OS Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS PG18) (Mycoplasma fermentans).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=496833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18;
RX PubMed=8613394; DOI=10.1128/iai.64.5.1800-1809.1996;
RA Theiss P., Karpas A., Wise K.;
RT "Antigenic topology of the P29 surface lipoprotein of Mycoplasma
RT fermentans: differential display of epitopes results in high-frequency
RT phase variation.";
RL Infect. Immun. 64:1800-1809(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18;
RX PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA Ishida N., Irikura D., Matsuda K., Sato S., Sone T., Tanaka M., Asano K.;
RT "Molecular cloning and expression of a novel cholinephosphotransferase
RT involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT fermentans.";
RL Curr. Microbiol. 58:535-540(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH69925.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U50826; AAC43988.1; -; Genomic_DNA.
DR EMBL; AP009608; BAH69925.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041594239.1; NC_021002.1.
DR AlphaFoldDB; Q49158; -.
DR SMR; Q49158; -.
DR STRING; 496833.MBIO_0660; -.
DR EnsemblBacteria; BAH69925; BAH69925; MBIO_0660.
DR KEGG; mfp:MBIO_0660; -.
DR PATRIC; fig|496833.3.peg.252; -.
DR eggNOG; COG1190; Bacteria.
DR HOGENOM; CLU_008255_6_0_14; -.
DR OrthoDB; 63621at2; -.
DR Proteomes; UP000006810; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00775; LysRS_core; 1.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..488
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152647"
FT BINDING 397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="T -> A (in Ref. 1; AAC43988)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="E -> D (in Ref. 1; AAC43988)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="G -> C (in Ref. 1; AAC43988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 56701 MW; A0BDF2B1FF794025 CRC64;
MTKYTEQEQI RRDKLEFYKK FDVVPFKKAY GLGKLSTSDE LNKKYGQFAR EELEAKKVKK
NISGRLITAR GPFLVLKDRK GTIQVYFNKK ENPELTKIVE TFDLGDILWV RGLLMKTHTG
EMTVRAQDIQ LLTKALKPLP DKFHGLTDTE ERYRHRYLDL ITNPESRNTF IMRTKIVQWI
RDYFNKLDYL EAETPFLHDY LSGAAAKPFT THHNSLNQDF VLRIATEIPL KKLVVGGFER
VYEMGRIFRN EGYDTTHNPE FTTIEFYEAY SNVEGMMNRT ETLIKELCKK IGKSKFVTNG
VEVDLSKPFK RVNMIDEVSK KTGKNFRKIT LEEAIEVAKA YKIKIEKFFT IGHIINALYE
ELVEPTLIQP TFLYGHPIEI SPLSAKSDDP RFTERAELFI NTKEYANMYT ELSDPIDQLE
RFESQLEEKN KGNDEASDID YDFVDALEYG MPPTGGCGIG IDRLVMLLTE TDSIRDVLLF
PTLKRIKK
