ID   C6AB48_BARGA            Unreviewed;       553 AA.
AC   C6AB48;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 91.
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   ECO:0000313|EMBL:ACS50415.1};
GN   OrderedLocusNames=Bgr_00230 {ECO:0000313|EMBL:ACS50415.1};
OS   Bartonella grahamii (strain as4aup).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS50415.1, ECO:0000313|Proteomes:UP000001489};
RN   [1] {ECO:0000313|EMBL:ACS50415.1, ECO:0000313|Proteomes:UP000001489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX   PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA   Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA   Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT   "Run-off replication of host-adaptability genes is associated with gene
RT   transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL   PLoS Genet. 5:E1000546-E1000546(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         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; CP001562; ACS50415.1; -; Genomic_DNA.
DR   RefSeq; WP_012754454.1; NC_012846.1.
DR   AlphaFoldDB; C6AB48; -.
DR   STRING; 634504.Bgr_00230; -.
DR   KEGG; bgr:Bgr_00230; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_2_0_5; -.
DR   OrthoDB; 9803151at2; -.
DR   Proteomes; UP000001489; 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: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           54..62
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   MOTIF           304..308
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   BINDING         307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   553 AA;  62758 MW;  DC3F6BCAFB72927E CRC64;
     MMRDQCDTLN LTPELKDAAS QSRTWPFEEA RKIIKRYEKT GYPDSVIFET GYGPSGLPHI
     GTFGEVARTT MVRHAFHILT ENKVKTKLLC FSDDMDGLRK VPENVPDRER MEHYLGQPLS
     RVPDPFGDDY PSFGAANNAR LRAFLDRFGF DYEFASATDY YHSGRFDETL LKILACYDKV
     MAIILPTLGA ERQATYSLFL PISPFSGKVL QVPMIERNVE KGTVTYIEPE TGETIETEVT
     GGKVKCQWKV DWAMRWTALG IDYEMAGKDL IDSTNLSSKI CKVLGGKSPE GFNYELFLDE
     KGQKISKSKG NGLTIDEWLT YAPTESLGLY MFSKPKTAKR LYFDVIPKAV DEYYAHLSAY
     GRQEWKERLN NPVWHIHNGC PPQVDLPVSF AMLLNLVSAS NAENAEVLWG FISRYAKGAN
     AQTYPELDQL VKFAIRYFDV FVKPNKKFRL PDESERTTLA QIDEKLANLP ETVDGNMLQN
     MLLDVARLTE RYQDHSKKSP EGGPGVSNVF FQMLYEVLLG QERGPRWGSF IALYGINEMR
     ALIAEALARP TEE
//