ID   SYI2_STAAU              Reviewed;        1024 AA.
AC   P41368;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   10-OCT-2018, entry version 112.
DE   RecName: Full=Isoleucine--tRNA ligase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   Name=ileS; Synonyms=mupR;
OS   Staphylococcus aureus.
OG   Plasmid pOX301.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=J2870; PLASMID=pOX301;
RX   PubMed=8067768; DOI=10.1128/AAC.38.5.1205;
RA   Hodgson J.E., Curnock S.P., Dyke K.G.H., Morris R., Sylvester D.R.,
RA   Gross M.S.;
RT   "Molecular characterization of the gene encoding high-level mupirocin
RT   resistance in Staphylococcus aureus J2870.";
RL   Antimicrob. Agents Chemother. 38:1205-1208(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 504-519 AND 550-609, AND
RP   FUNCTION.
RC   STRAIN=J2870;
RX   PubMed=1903747; DOI=10.1016/0378-1097(91)90550-T;
RA   Dyke K.G.H., Curnock S.P., Golding M., Noble W.C.;
RT   "Cloning of the gene conferring resistance to mupirocin in
RT   Staphylococcus aureus.";
RL   FEMS Microbiol. Lett. 61:195-198(1991).
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile) (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Confers high-level resistance to the antibiotic
CC       mupirocin (pseudomonic acid A), an Ile-analog that competitively
CC       inhibits activation by Ile-tRNA synthetase, thus inhibiting
CC       protein biosynthesis. {ECO:0000269|PubMed:1903747,
CC       ECO:0000269|PubMed:8067768}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)) (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 2 subfamily. {ECO:0000305}.
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DR   EMBL; X75439; CAA53189.1; -; Genomic_DNA.
DR   EMBL; X59478; CAA42080.1; -; Genomic_DNA.
DR   EMBL; X59477; CAA42079.1; -; Genomic_DNA.
DR   RefSeq; WP_012263521.1; NG_056478.1.
DR   RefSeq; YP_001653102.1; NC_010279.1.
DR   ProteinModelPortal; P41368; -.
DR   SMR; P41368; -.
DR   GeneID; 5857592; -.
DR   BRENDA; 6.1.1.5; 3352.
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:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 2.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; Antibiotic resistance; ATP-binding;
KW   Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Plasmid;
KW   Protein biosynthesis; Zinc.
FT   CHAIN         1   1024       Isoleucine--tRNA ligase.
FT                                /FTId=PRO_0000098562.
FT   MOTIF        42     52       "HIGH" region.
FT   MOTIF       585    589       "KMSKS" region.
FT   BINDING     588    588       ATP. {ECO:0000250}.
FT   CONFLICT    519    519       P -> R (in Ref. 2; CAA42079).
FT                                {ECO:0000305}.
FT   CONFLICT    591    593       GNV -> ETF (in Ref. 2; CAA42080).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1024 AA;  118876 MW;  56ECD232CA0C8430 CRC64;
     MTKKYLNTQN EISAFWNTQK IFKKSIDNRK GQESFVFYDG PPTANGLPHA GHVLGRVIKD
     LVARLKTMQG FYVERKAGWD THGLPVELEV EKKIGIKGKQ DIEKYGIENF INECKKSVFN
     YEKEWRDFSK DLGYWVDMDS PYITLENNYI ESVWNILSTF HKKGLLYKGH KVTPYCTHDQ
     TALSSHEVAQ GYKNVKDLSA VVKFQLTNSK DTYFLSWTTT PWTLPANVAL AINKDLNYSK
     IRVENEYYIL ATDLINSIIT EKYEIIDTFS GSNLINLKYI PPFESDGLVN AYYVVDGEFV
     TNSEGTGIVH IAPAHGEDDY QLVLERDLDF LNVITREGVY NDRFPELVGN KAKNSDIEII
     KLLSKKQLLY KKQKYEHNYP HCWRCGNPLI YYAMEGWFIK TTNFKNEIIN NNNNIEWFPS
     HIKEGRMGNF LENMVDWNIG RNRYWGTPLN VWICNDCNHE YAPSSIKDLQ NNSINKIDED
     IELHRPYVDN ITLSCPKCNG KMSRVEEVID VWFDSGSMPF AQHHYPFDNQ KIFNQHFPAD
     FIAEGVDQTR GWFYSLLVIS TILKGKSSYK RALSLGHILD SNGKKMSKSK GNVINPTELI
     NKYGADSLRW ALISDSAPWN NKRFSENIVA QTKSKFIDTL DNIYKFYNMY NKIDHYNPNN
     EITKSRNTLD NWALSRLNTL IKESNIYVNN YDFTSAARLI NEYTNTISNW YIGDSRGRFW
     EQGISNDKKD AYNTLYEILT TLSRLVAPFV PFISEKIHYN LTGKSVHLQD YPQYKESFIN
     QALEDEMHTV IKIVELSRQA RKNADLKIKQ PLSKMVIKPN SQLNLSFLPN YYSIIKDELN
     IKNIELTDNI NDYITYELKL NFSSVGPKLG NKTKNIQTLI DSLSEYDKKS LIESNNFKSL
     SSDAELTKDD FIIKTLPKDS YQLSEDNDCV ILLDKNLSPE LIREGHAREL IRLIQQLRKK
     KNLPINQRID IYIGVTGELL ESIKTNKNMF KENFVIKNIH LNVIDEYENT IHFNNKEIKI
     SLLY
//