ID   SYK_CAUSK               Reviewed;         552 AA.
AC   B0T2A6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; OrderedLocusNames=Caul_0137;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000927; ABZ69275.1; -; Genomic_DNA.
DR   RefSeq; WP_012284233.1; NC_010338.1.
DR   AlphaFoldDB; B0T2A6; -.
DR   SMR; B0T2A6; -.
DR   STRING; 366602.Caul_0137; -.
DR   EnsemblBacteria; ABZ69275; ABZ69275; Caul_0137.
DR   KEGG; cak:Caul_0137; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_2_0_5; -.
DR   OMA; DWPMRWA; -.
DR   OrthoDB; 256927at2; -.
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:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR37940; PTHR37940; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00467; lysS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..552
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_1000199266"
FT   MOTIF           71..79
FT                   /note="'HIGH' region"
FT   MOTIF           319..323
FT                   /note="'KMSKS' region"
FT   BINDING         322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   552 AA;  61290 MW;  8F50A04632227276 CRC64;
     MFQGLSPLAR DARAWPFEQA RVLLARILRL RLSDAERDLA SVLIHSGKAD EAVRTFPALA
     KPVILETGYG PSGLPHLGTF GEVARTTMVR NAFRALTDDA IKTRLIAFSD DMDGLRKVPD
     NIENKQPLIE DLGKPLTVVR DPFGTHDSFG AHNNARLRAF LDGFGFEYEF VSSTDCYKGG
     LFDETLLTAL ARFDAIQKVM LPTLGEERRA SYSPFLPISP STGKVLQVPT LERDVDKGTI
     VFQDEDGSKV EVPVTGGHVK MQWKPDWAMR WTALGVDYEM SGKDLIDSVK ASGQICKALG
     GVPPEGFNYE LFLDENSQKI SKSKGNGLSM EDWLRYGAPE SLSYYMFQSP KSAKKLYFDV
     IPKATDEYLQ QLDAYPKQEP AKQLDNPVWH VHSGRPPQYG SPVSFSLMLN LVSAANASDK
     EILWGFLSRY IPGATPQSQP LLDRLAGYAI NYYEDFVKPS KVFRAPDDKE RAAMLDLLGR
     LKALPSDCQD AELIQNEVFA VGKDHGFDPL RAWFQALYEV LLGQSQGPRF GSFAAIFGLD
     RTTALIAEKL AV