ID SYL_NEIG1 Reviewed; 876 AA.
AC Q5FAJ3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=NGO0006;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; AE004969; AAW88778.2; -; Genomic_DNA.
DR RefSeq; WP_025456399.1; NC_002946.2.
DR RefSeq; YP_207190.2; NC_002946.2.
DR PDB; 6YKK; X-ray; 2.24 A; A=1-876.
DR PDB; 6YKL; X-ray; 2.27 A; A=1-876.
DR PDB; 6YKN; X-ray; 2.63 A; A=1-876.
DR PDB; 6YKO; X-ray; 2.21 A; A=1-876.
DR PDB; 6YKQ; X-ray; 1.94 A; A=1-876.
DR PDB; 6YKS; X-ray; 1.97 A; A=1-876.
DR PDB; 6YKT; X-ray; 2.32 A; A=1-876.
DR PDB; 6YKU; X-ray; 2.14 A; A=1-876.
DR PDB; 6YKV; X-ray; 2.43 A; A=1-876.
DR PDB; 6YKW; X-ray; 2.46 A; A=1-876.
DR PDB; 6YKX; X-ray; 2.41 A; A=1-876.
DR PDB; 7A0P; X-ray; 2.18 A; A=1-876.
DR PDB; 7AP2; X-ray; 2.25 A; A=1-876.
DR PDBsum; 6YKK; -.
DR PDBsum; 6YKL; -.
DR PDBsum; 6YKN; -.
DR PDBsum; 6YKO; -.
DR PDBsum; 6YKQ; -.
DR PDBsum; 6YKS; -.
DR PDBsum; 6YKT; -.
DR PDBsum; 6YKU; -.
DR PDBsum; 6YKV; -.
DR PDBsum; 6YKW; -.
DR PDBsum; 6YKX; -.
DR PDBsum; 7A0P; -.
DR PDBsum; 7AP2; -.
DR AlphaFoldDB; Q5FAJ3; -.
DR SMR; Q5FAJ3; -.
DR STRING; 242231.NGO_0006; -.
DR KEGG; ngo:NGO_0006; -.
DR PATRIC; fig|242231.10.peg.7; -.
DR HOGENOM; CLU_004427_0_0_4; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..876
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334780"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 634..638
FT /note="'KMSKS' region"
FT BINDING 637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
FT HELIX 7..21
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6YKV"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6YKV"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 226..236
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6YKL"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 404..417
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 420..427
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6YKL"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 483..486
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 513..516
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 529..535
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 537..544
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 550..564
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:7A0P"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 626..634
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 637..640
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 645..652
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 654..664
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:6YKV"
FT HELIX 675..697
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 714..735
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 740..755
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 762..779
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 784..794
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 799..802
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 809..812
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 820..823
FT /evidence="ECO:0007829|PDB:6YKQ"
FT HELIX 841..847
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 865..867
FT /evidence="ECO:0007829|PDB:6YKQ"
FT TURN 868..870
FT /evidence="ECO:0007829|PDB:6YKQ"
FT STRAND 871..874
FT /evidence="ECO:0007829|PDB:6YKQ"
SQ SEQUENCE 876 AA; 98049 MW; E2B73DC55263D03E CRC64;
MQEHYQPAAI EPAAQKKWDD ARISNVSEDA SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
VLSRFKLLNG FNVMQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIEYMKT QLKSLGFAID
WEREVATCKP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALIEKREIPM YYFKITDYAE ELLNDLDKLE HWPEQVKTMQ RNWIGKSRGM TVRFAVSDDS
KQGLEGDYAK FLQVYTTRPD TLMGATYVAV AAEHPLATAA AADKPELQAF IAECKAGSVA
EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFAAK
YNLPKKQVIA VGDNAFDANR WQEWYGDKEN GVLVNSGDLD GLDFQTAFDA VAAKLQSQGA
GEPKTQYRLR DWGISRQRYW GCPIPIVHCE KCGDVPVPAD QLPVVLPENV VPDGMGSPLA
KMPEFYETSC PCCGGAAKRE TDTMDTFMES SWYFFRYMSP KFSDGMVSAE SAKYWGAVDQ
YIGGIEHAIL HLLYARFFTK LMRDEGLVNV DEPFERLLTQ GMVVCETYYR ENDKGGKDWI
NPADVELTFD DKGRPVSAVL KADGLPVVIS GTEKMSKSKN NGVDPQELIN AYGADTARLF
MMFAAPPEQS LEWSDSGVEG AHRFLRRLWR TVYEYLKQGG AVKAFAGNQD GLSKELKDLR
HKLHSTTAKV SDDYGRRQQF NTAIAAVMEL LNQYDKTDTG SEQGRAVAQE VLEAAVRLLW
PIVPHICETL WSELNGAKLW EAGWPTVDEA ALVKSEIEVM VQVNGKLRGK ITVAADASKA
DLEAAALANE GAVKFMEGKP AKKIIVVPGR LVNIVV
//
