SYW_MYCPN
ID SYW_MYCPN Reviewed; 346 AA.
AC P75510;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140};
DE Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140};
GN Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=MPN_265;
GN ORFNames=MP568;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000255|HAMAP-Rule:MF_00140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00140};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00140}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00140}.
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DR EMBL; U00089; AAB96216.1; -; Genomic_DNA.
DR PIR; S73894; S73894.
DR RefSeq; NP_109953.1; NC_000912.1.
DR RefSeq; WP_010874622.1; NC_000912.1.
DR PDB; 2YY5; X-ray; 2.55 A; A/B/C/D=1-346.
DR PDBsum; 2YY5; -.
DR AlphaFoldDB; P75510; -.
DR SMR; P75510; -.
DR IntAct; P75510; 2.
DR STRING; 272634.MPN_265; -.
DR EnsemblBacteria; AAB96216; AAB96216; MPN_265.
DR KEGG; mpn:MPN_265; -.
DR PATRIC; fig|272634.6.peg.284; -.
DR HOGENOM; CLU_029244_1_1_14; -.
DR OMA; GWGQFKP; -.
DR BioCyc; MPNE272634:G1GJ3-416-MON; -.
DR EvolutionaryTrace; P75510; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 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..346
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136648"
FT MOTIF 11..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 200..204
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 10..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 18..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 140
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 152..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 200..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:2YY5"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 52..68
FT /evidence="ECO:0007829|PDB:2YY5"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2YY5"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:2YY5"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 156..173
FT /evidence="ECO:0007829|PDB:2YY5"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2YY5"
FT TURN 186..190
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:2YY5"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 282..305
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 309..338
FT /evidence="ECO:0007829|PDB:2YY5"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2YY5"
SQ SEQUENCE 346 AA; 39079 MW; 66CF4FFCCE9C2F95 CRC64;
MMKRALTGIQ ASGKQHLGNY LGVMQSLIEL QEQCQLFVFV ADLHSITVDF QPQALKQNNF
DLVRTLLAVG LDPQKACLFL QSDLLEHSMM GYLMMVQSNL GELQRMTQFK AKKAEQTRNP
NGTLNIPTGL LTYPALMAGD ILLYQPDIVP VGNDQKQHLE LTRDLAQRIQ KKFKLKLRLP
QFVQNKDTNR IMDLFDPTKK MSKSSKNQNG VIYLDDPKEV VVKKIRQATT DSFNKIRFAP
KTQPGVTNML TILKALLKEP VNQSLTNQLG NDLEAYFSTK SYLDLKNALT EATVNLLVNI
QRKREQISRE QVFNCLQAGK NQAQATARTT LALFYDGFGL GSQNIK
