ID A0A1B1Z1Y8_9BACI Unreviewed; 514 AA.
AC A0A1B1Z1Y8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=ABE41_005375 {ECO:0000313|EMBL:ANX11430.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX11430.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX11430.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX11430.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-2016) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; CP016761; ANX11430.1; -; Genomic_DNA.
DR RefSeq; WP_066287259.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z1Y8; -.
DR STRING; 255247.ABE41_005375; -.
DR KEGG; far:ABE41_005375; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000077412; 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 Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 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; IPR042078; Lys-tRNA-ligase_SC_fold.
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}; Reference proteome {ECO:0000313|Proteomes:UP000077412}.
FT MOTIF 29..37
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 279..283
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 514 AA; 60332 MW; 84C872C11828DBA3 CRC64;
MHWAYRIAEE LIRKHPNHDT FVCASGISPS GSVHIGNFRE VVTTYFVVKA LQQMGKKTRF
IFSWDDFDRF RKVPKNLDPS FEQYIGMPYA EIPCPFGCHS TYAEHFEKEF EESLLQFGIV
PEFIYQSEEY RAKRYNVQIL HVLENRKQIY DILMAYKTAK PNEQERENFY PVNVYCDRCR
KDTVSITSFQ ECHLSYTCSC GHSNTVEIME ATNMKLNWKV DWPMRWMVEN VVFEPGGRDH
SSETGSYRVS KEIAIEIFYH QAPTYKPYEF ISIKGTGEKM SSSSGNNITP EELLRVYTPE
IILFMFAKYQ PNSAFHIGLD EDVIRNYTEY ERFREVDPAQ LKEEIKAALY FSVKKEKLLN
GPKFAQVASI LPLVNFDALL VKDVLNRIGE AFSLDEIQKV CERAEYWLRN WCPEKVLNIN
NQKYHVYYEM LTSVEKEWVH GFTEVLKNGP ALDEELMRNV YDICHDDNPK VKRNNQKRLF
QIIYQLILNN NSGPRIPLLV HAVGKERLLS LLDF
//
