ID   SYN_STRPN               Reviewed;         447 AA.
AC   Q97PR0;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=SP_1542;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00534};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   -!- INTERACTION:
CC       Q97PR0; Q97QS2: eno; NbExp=2; IntAct=EBI-2207302, EBI-2207206;
CC       Q97PR0; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207302, EBI-2207053;
CC       Q97PR0; Q97NV3: groES; NbExp=2; IntAct=EBI-2207302, EBI-2206949;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR   EMBL; AE005672; AAK75630.1; -; Genomic_DNA.
DR   PIR; E95179; E95179.
DR   RefSeq; WP_000167151.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97PR0; -.
DR   SMR; Q97PR0; -.
DR   IntAct; Q97PR0; 3.
DR   STRING; 170187.SP_1542; -.
DR   EnsemblBacteria; AAK75630; AAK75630; SP_1542.
DR   KEGG; spn:SP_1542; -.
DR   eggNOG; COG0017; Bacteria.
DR   OMA; DNMDLAE; -.
DR   PhylomeDB; Q97PR0; -.
DR   BioCyc; SPNE170187:G1FZB-1560-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00457; asnS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..447
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_0000176460"
SQ   SEQUENCE   447 AA;  51067 MW;  D098EDC458500D8D CRC64;
     MTKRVTIIDV KDYVGQEVTI GAWVANKSGK GKIAFLQLRD GTAFFQGVAF KPNFVEKFGE
     EVGLEKFDVI KRLSQETSVY VTGIVKEDER SKFGYELDIT DIEVIGESQD YPITPKEHGT
     DFLMDNRHLW LRSRKQVAVL QIRNAIIYAT YEFFDKNGFM KFDSPILSGN AAEDSTELFE
     TDYFGTPAYL SQSGQLYLEA GAMALGRVFD FGPVFRAEKS KTRRHLTEFW MMDAEYSYLT
     HDESLDLQEA YVKALLQGVL DRAPQALETL ERDTELLKRY IAEPFKRITY DQAIDLLQEH
     ENDEDADYEH LEHGDDFGSP HETWISNHFG VPTFVMNYPA AIKAFYMKPV PGNPERVLCA
     DLLAPEGYGE IIGGSMREED YDALVAKMDE LGMDRTEYEF YLDLRKYGTV PHGGFGIGIE
     RMVTFAAGTK HIREAIPFPR MLHRIKP