SYW_BACSU
ID SYW_BACSU Reviewed; 330 AA.
AC P21656;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=BSU11420;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3149612; DOI=10.1016/0378-1119(88)90518-5;
RA Chow K.C., Wong T.F.;
RT "Cloning and nucleotide sequence of the structural gene coding for Bacillus
RT subtilis tryptophanyl-tRNA synthetase.";
RL Gene 73:537-543(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1-32.
RX PubMed=2494170; DOI=10.1016/s0021-9258(18)83740-1;
RA Xu Z.J., Love M.L., Ma L.Y.Y., Blum M., Bronskill P.M., Bernstein J.,
RA Grey A.A., Hofmann T., Camerman N., Wong J.T.F.;
RT "Tryptophanyl-tRNA synthetase from Bacillus subtilis. Characterization and
RT role of hydrophobicity in substrate recognition.";
RL J. Biol. Chem. 264:4304-4311(1989).
RN [4]
RP MUTAGENESIS OF TRP-92.
RX PubMed=1577751; DOI=10.1016/s0021-9258(19)50401-x;
RA Chow K.C., Xue H., Shi W., Wong J.T.;
RT "Mutational identification of an essential tryptophan in tryptophanyl-tRNA
RT synthetase of Bacillus subtilis.";
RL J. Biol. Chem. 267:9146-9149(1992).
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; M24068; AAA22874.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12999.1; -; Genomic_DNA.
DR PIR; JT0481; YWBS.
DR RefSeq; NP_389024.1; NC_000964.3.
DR RefSeq; WP_003245134.1; NZ_JNCM01000035.1.
DR PDB; 3PRH; X-ray; 2.80 A; A/B=1-329.
DR PDBsum; 3PRH; -.
DR AlphaFoldDB; P21656; -.
DR SMR; P21656; -.
DR STRING; 224308.BSU11420; -.
DR jPOST; P21656; -.
DR PaxDb; P21656; -.
DR PRIDE; P21656; -.
DR EnsemblBacteria; CAB12999; CAB12999; BSU_11420.
DR GeneID; 939361; -.
DR KEGG; bsu:BSU11420; -.
DR PATRIC; fig|224308.179.peg.1228; -.
DR eggNOG; COG0180; Bacteria.
DR InParanoid; P21656; -.
DR OMA; GWGQFKP; -.
DR PhylomeDB; P21656; -.
DR BioCyc; BSUB:BSU11420-MON; -.
DR SABIO-RK; P21656; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; 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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..330
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136602"
FT MOTIF 11..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 193..197
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 133
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 145..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 193..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MUTAGEN 92
FT /note="W->F,A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1577751"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:3PRH"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:3PRH"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 52..68
FT /evidence="ECO:0007829|PDB:3PRH"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3PRH"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:3PRH"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3PRH"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:3PRH"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 266..291
FT /evidence="ECO:0007829|PDB:3PRH"
FT HELIX 295..323
FT /evidence="ECO:0007829|PDB:3PRH"
SQ SEQUENCE 330 AA; 37197 MW; 31927E2BC6320544 CRC64;
MKQTIFSGIQ PSGSVTLGNY IGAMKQFVEL QHDYNSYFCI VDQHAITVPQ DRLELRKNIR
NLAALYLAVG LDPEKATLFI QSEVPAHAQA GWMMQCVAYI GELERMTQFK DKSKGNEAVV
SGLLTYPPLM AADILLYGTD LVPVGEDQKQ HLELTRNLAE RFNKKYNDIF TIPEVKIPKV
GARIMSLNDP LKKMSKSDPN QKAYITLLDE PKQLEKKIKS AVTDSEGIVK FDKENKPGVS
NLLTIYSILG NTTIEELEAK YEGKGYGEFK GDLAEVVVNA LKPIQDRYYE LIESEELDRI
LDEGAERANR TANKMLKKME NAMGLGRKRR
