SYI_CHLPN
ID SYI_CHLPN Reviewed; 1043 AA.
AC Q9Z972; Q9JQK2; Q9K221;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
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=CPn_0109, CP_0665, CpB0110;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD18262.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38477.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98320.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98043.1; -; Genomic_DNA.
DR PIR; C81552; C81552.
DR PIR; E72118; E72118.
DR PIR; F86504; F86504.
DR RefSeq; NP_224317.1; NC_000922.1.
DR RefSeq; WP_010882759.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z972; -.
DR SMR; Q9Z972; -.
DR STRING; 115711.CP_0665; -.
DR EnsemblBacteria; AAD18262; AAD18262; CPn_0109.
DR EnsemblBacteria; AAF38477; AAF38477; CP_0665.
DR KEGG; cpa:CP_0665; -.
DR KEGG; cpj:ileS; -.
DR KEGG; cpn:CPn_0109; -.
DR KEGG; cpt:CpB0110; -.
DR PATRIC; fig|115713.3.peg.123; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_0; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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; 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 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; 1.
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; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..1043
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098528"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 591..595
FT /note="'KMSKS' region"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
FT CONFLICT 384
FT /note="H -> Y (in Ref. 2; AAF38477)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="R -> H (in Ref. 4; AAP98043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1043 AA; 120287 MW; 08ABB8B9364E640C CRC64;
MTADEVGKNS FAKKEEQVLK FWKDNQIFEK SLQNRQGKTL YSFYDGPPFA TGLPHYGHLL
ASTIKDVVGR YATMDGYYVP RRFGWDCHGV PVEYEVEKSL SLTAPGAIED FGIASFNEEC
RKIVFRYVHE WEYYINRIGR WVDFSSTWKT MDASFMESVW WVFQSLYNQG LVYEGTKVVP
FSTALGTPLS NFEASQNYKE VDDPSLVVRM PLQNDSASLL VWTTTPWTLP SNMAIAVGET
LVYVRIQDKK SGEQWILSQG CVSRWFSNPE EFVILESFSG KDLVGRTYEP PFTFFQSKRE
EGAFRVIAAS FVEESEGTGV VHMAPAFGEG DFLVCKENHV PLVCPVDAHG SFTEEIPQYQ
GQYIKHADKE IIKFLKKEGR IFYHGTVKHR YPFCWRTDTP LIYKAVNSWF VAVEKIKDKM
LRANSSIHWV PEHIQEGRFG KWLEGARDWA ISRNRYWGTP IPIWKSADGE ILVVGSIREL
EELTGTQITD IHRHFIDDLN IVKDGKPFHR IPYVFDCWFD SGAMPYAQNH YPFENQKETE
EAFPADFIAE GLDQTRGWFY TLTVISAILF DRPAFRNAIV NGIILAEDGN KMSKRLNNYP
SPKYVLDTYG ADALRLYLLH SVVVKAEDLR FSDKGIEGVL KQILLPLTNV LSFFNTYAEL
YGFDPKSQDI EPAYTEIDQW ILSNLYSVVG KVRESMSQYH LNFAVEPFVT FIDDLTNWYI
RRCRRRFWEA EDTPDRRAAF STLYEVLTVF CKVIAPFVPF LAEDIYQKLK LEKEPESVHL
CDFPQVEMDK ILPDLEKRMH DIREIVGLGH SLRKEHKLKV RQPLANFYVV GSKDRLSLLK
TFEGLIAEEL NVKNVIFYEE APSFIYTTVK PNFRMLGKKV GSKMKEVQKA LSELPNNAID
KLIQEETWVL TIDDREIALD GDDVVICRHT DPGYIARSSA LFSVILDCQL REPLIVEGIA
RELVNKINTM RRNQQLHVSD RIALRIKTTE AVHRAFLDYE NYICEETLII AYDFTQDSDF
QGENWDINGH ATQIEITVSS IDS
