SYW_CHLTR
ID SYW_CHLTR Reviewed; 346 AA.
AC O84589;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=CT_585;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC68187.1; -; Genomic_DNA.
DR PIR; B71496; B71496.
DR RefSeq; NP_220100.1; NC_000117.1.
DR RefSeq; WP_009871951.1; NC_000117.1.
DR PDB; 6NCR; X-ray; 1.75 A; A/B=1-346.
DR PDBsum; 6NCR; -.
DR AlphaFoldDB; O84589; -.
DR SMR; O84589; -.
DR STRING; 813.O172_03205; -.
DR EnsemblBacteria; AAC68187; AAC68187; CT_585.
DR GeneID; 884362; -.
DR KEGG; ctr:CT_585; -.
DR PATRIC; fig|272561.5.peg.637; -.
DR HOGENOM; CLU_029244_0_1_0; -.
DR InParanoid; O84589; -.
DR OMA; GWGQFKP; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
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_0000136620"
FT MOTIF 12..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 201..205
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 19..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 143
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 155..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 201..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:6NCR"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:6NCR"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6NCR"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:6NCR"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:6NCR"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6NCR"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6NCR"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 274..301
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 304..332
FT /evidence="ECO:0007829|PDB:6NCR"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:6NCR"
SQ SEQUENCE 346 AA; 39492 MW; 5FB8C0A86CE172CE CRC64;
MKKKRVLTGD RPTGKLHLGH WIGSIMNRLQ LQNDSRYDCF FIIADLHTLT TKTRKEEILQ
IDNHIYDVLA DWLSVGIDPE KSAIYLQSAI PEIYELNLIF SMLTPLNHIM GIPSIKEMAR
NASLNEESLS HGLIGYPVLQ SADILLAKAH LVPVGKDNEA HVELTRDIAK TFNRLYGEVF
PEPDILQGEL TALVGTNGQG KMSKSANNAI YLSDDAKTVQ EKIRKLYTDP NRIHATTPGR
VEGNPLFIYH DLFNPHKEEV EEFKTRYRQG CIRDVEVKAR LAEEINLFLN PFREKRSELV
AQPKFLEEAL QQGTEKMRTV ARETMEEVHD HLGLSRKWRT ILASSK
