ID   Q07TP1_RHOP5            Unreviewed;       546 AA.
AC   Q07TP1;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   OrderedLocusNames=RPE_0736 {ECO:0000313|EMBL:ABJ04693.1};
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ04693.1};
RN   [1] {ECO:0000313|EMBL:ABJ04693.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53 {ECO:0000313|EMBL:ABJ04693.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC         Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
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DR   EMBL; CP000463; ABJ04693.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07TP1; -.
DR   STRING; 316055.RPE_0736; -.
DR   KEGG; rpe:RPE_0736; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_2_0_5; -.
DR   OrthoDB; 9803151at2; -.
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; HUPs; 2.
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   NCBIfam; TIGR00467; lysS_arch; 1.
DR   PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00177};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00177}.
FT   MOTIF           51..59
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   MOTIF           300..304
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   546 AA;  60716 MW;  37639DB03E7C97B7 CRC64;
     MSTTDLAQNP AELRALAEQS NAWPFEQAKA LVARLNKAPK DEVLFETGYG PSGLPHIGTF
     GEVARTTMVR HAFRVLTEDK IKTRLIAFSD DMDGLRKVPD NVPNKELLSQ HLGKSLSSVP
     DPFGTHESFG AHNNARLRAF LDTFSFDYEF ASATDYYKSG RFDATLLKVL QRLDKVMAIM
     LPSLREERAA SYSPFLPICP RTGVVLQVPI AAHDVAAGTI SYDDPETNER VTLPVTGGHC
     KLQWKPDWAM RWTALGIDYE MAGKDLIDSV KLSGKICQAI GGTPPEGFNY ELFLDDKGQK
     ISKSKGNGLT IDEWLRYASP ESLSLFMYRE PKAAKRLYFD VIPRNVDDYQ QFLDGFSRQD
     AKQQLSNPVW HIHAGQPPKA DMPVTFQLLL TLVSSSNAEN AATLWGFIGR YRPGVSPQTH
     PKLDAMVGYA INYYRDFVAP TKSFREPTDQ ERAALQDLRD ALSHLPAEST AEAIQDVVYE
     IGRREPFLDH KKAAKDGKPG VSLDWFNMLY QVLLGQEKGP RFGSFVAVYG LANAVAMIDG
     ALARSA
//