ID   SYI_CHLMU               Reviewed;        1036 AA.
AC   Q9PL20;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   28-JAN-2026, entry version 137.
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};
GN   OrderedLocusNames=TC_0288;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
OC   Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC         COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         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; AE002160; AAF39156.1; -; Genomic_DNA.
DR   PIR; F81719; F81719.
DR   RefSeq; WP_010230051.1; NC_002620.2.
DR   AlphaFoldDB; Q9PL20; -.
DR   SMR; Q9PL20; -.
DR   GeneID; 1246458; -.
DR   KEGG; cmu:TC_0288; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   CDD; cd00818; IleRS_core; 1.
DR   FunFam; 3.40.50.620:FF:000241; Isoleucine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000133; Isoleucyl-tRNA synthetase, cytoplasmic; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 2.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1036
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098527"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           589..593
FT                   /note="'KMSKS' region"
FT   BINDING         592
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1036 AA;  118950 MW;  69E6B05FD54D5E8D CRC64;
     MDNEDKVSFP AKEEKVLTFW KEQNIFQKTL ENRDGSPTFS FYDGPPFATG LPHYGHLLAG
     TIKDVVCRYA TMDGHYVPRR FGWDCHGVPV EYEVEKSLGL TEPGAIDRFG IANFNEECRK
     IVFRYVDEWK YFVDRIGRWV DFSATWKTMD LSFMESVWWV FHSLYKQGLV YEGTKVVPFS
     TKLGTPLSNF EAGQNYKEVD DPSVVAKFAL QDDQGILLAW TTTPWTLVSN MALAVHPGLT
     YVRIQDKESG EEYILGQESL ARWFPDRESY KWIGQLSGES LVGRRYCPLF PYFQDQQDRG
     AFRVIPADFI EESEGTGVVH MAPAFGEADF FACQEHNVPL VCPVDNQGCF TSEVTDFVGE
     YIKFADKGIA RRLKNENKLF YQGTIRHRYP FCWRTDSPLI YKAVNSWFVS VEKVKHKMLK
     ANESIHWTPG HIKHGRFGKW LEGARDWAIS RNRYWGTPIP IWRSEDGELL VIRSIQELEE
     LSGQKIVDLH RHFIDEIVIH KNGKSFHRIP YVFDCWFDSG AMPYAQNHYP FERAEETEAR
     FPADFIAEGL DQTRGWFYTL TVIAAALFDQ PAFKNVIVNG IVLAEDGNKM SKRLNNYPSP
     KKIMDTYGAD ALRLYLLNSV VVKAEDLRFS DKGVEAVLKQ VLLPLSNALA FYKTYAELYG
     FSPNETTDLE LAEIDRWILS SLYSLVGKTR ENMAQYDLHA AVSPFIDFIE DLTNWYIRRS
     RRRFWESEDS PDRRAAFATL YEVLMVFSKI IAPFIPFTAE DMYQQLRVET DPESVHLCDF
     PHVVLEKILP DLEKKMQDIR EIVALGHSLR KEHKLKVRQP LQHMYIVGAK ERMAALAQVD
     SLIGEELNVK EVHFCSETPE YVTTLVKPNF RSLGKRVGNR LPEIQKALAG LSQEQIQAFM
     HNGFMVLSLG EETISLNEED ITVSWEAAPG FVARSSASFV AILDCQLTSP LIMEGIAREI
     VNKINTMRRN GKLHVSDRIA IRLHAPKIVQ EAFSQYEEYI CEETLTTSVS FIDDKEGEEW
     DVNGHAVSLS LEVIGH
//