ID   SYI_BORGP               Reviewed;        1042 AA.
AC   Q65ZU1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=BG0858;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC       can inadvertently accommodate and process structurally similar amino
CC       acids such as valine, to avoid such errors it has two additional
CC       distinct tRNA(Ile)-dependent editing activities. One activity is
CC       designated as 'pretransfer' editing and involves the hydrolysis of
CC       activated Val-AMP. The other activity is designated 'posttransfer'
CC       editing and involves deacylation of mischarged Val-tRNA(Ile).
CC       {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated valine is translocated from the
CC       active site to the editing site, which sterically excludes the
CC       correctly activated isoleucine. The single editing site contains two
CC       valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC       tRNA(Ile)). {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; CP000013; AAU07680.1; -; Genomic_DNA.
DR   RefSeq; WP_011194124.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q65ZU1; -.
DR   SMR; Q65ZU1; -.
DR   STRING; 290434.BG0858; -.
DR   EnsemblBacteria; AAU07680; AAU07680; BG0858.
DR   KEGG; bga:BG0858; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_12; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002276; Chromosome.
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   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
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   PANTHER; PTHR42780; PTHR42780; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..1042
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098526"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           594..598
FT                   /note="'KMSKS' region"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1042 AA;  122408 MW;  6389CBC417E852C4 CRC64;
     MFKKVENKAN FPKIEEKILK FWNDNKIFEK SMEQREGCEE FTFYDGPPFA TGLPHFGHFV
     PNTIKDIIPR YQTMKGKYVK RNFGWDTHGL PVEYEVEKKL GISGKYEIEN YGIENFNKEC
     KKIVLRYTEE WKNIILRLGR WVDFEKGYKT MDISFMESVW WVFKNLYNKG LIYESYYVLP
     YSPKLATPLS NFEVNLGEYK EVNDPSLTIK FKIKDKNEYL LAWTTTPWTL PSNLGIAVGK
     EIEYSKIFDK KKEEILILGS KKINSYFDDE NAYTIIEKFK GSQLQGIEYE PIFNYFLEQK
     DKGAFKVHTA DYITTDDGTG IVHIAPFGEE DYRVLKKHTN VDIIDPLDAE CKFTNRVKDF
     KGLFVKDADK KIIENLKLRN FLFKRENYLH RYPFCYRTNY PIIYRPISSW FVNVEKIKTQ
     LLEVNEKINW MPAHLKKGRF GKWLENAKDW AISRNRFWGN PIPIWICSKT GKKICVGSRK
     ELEELSGQKI EDLHKDKIDK ITWPSKDGGT FIRTSEVLDC WFESGAMPYA SNHYPFANES
     NFKNIFPADF IAEGLDQTRG WFYTLTILGT SLFENTAFKN VIVNGLVLSS DGRKMSKSFK
     NYTDPMEVIN TFGADALRLY LIMSPVVKAD DLKYSDNGVR DVLKNIIIPI WNAYSFFTTY
     AIIDKFKPTK NLSLVKSNNL DKWIISELES LKKILNKEID KYNLTKSIES LLEFIDKLNN
     WYIRRSRRRF WKSENDKDKN DAYETLYYAI KTLMILLAPF IPFITEEIYQ NLKTDEDKQS
     IHLNDYPKAN ENFIDKTIEE KINLARKITS MARSLRSLHN IKIRMPISTI YVVTKNQNEQ
     NMLIEMQEII LDEINVKEMK IKSNEEELIT YKAKANFKEL GKKLGKDMKT VSIEISKLKN
     EDIIKIINGI SHEIKVDNAK YYLSLNDIIL ERDEKDNLKV INEESITIGI DSLITQELYL
     EGLTREFVRQ IQNLRKEKNF DVSDRINLYI ENNATLEEIL NKFEKYIKTE TLALNIILNK
     SKLEKKINLD NDIFTIIGIE KC