ID   SYI_TREPA               Reviewed;        1091 AA.
AC   O83466;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 141.
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=TP_0452;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; 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; AE000520; AAC65439.1; -; Genomic_DNA.
DR   PIR; E71322; E71322.
DR   RefSeq; WP_010881901.1; NC_021490.2.
DR   AlphaFoldDB; O83466; -.
DR   SMR; O83466; -.
DR   IntAct; O83466; 3.
DR   STRING; 243276.TP_0452; -.
DR   EnsemblBacteria; AAC65439; AAC65439; TP_0452.
DR   KEGG; tpa:TP_0452; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_12; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000811; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..1091
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098569"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1091 AA;  124242 MW;  30FCAE18C6F301A2 CRC64;
     MYTPVDPKVD FVAQERRILA FWRERRVFEQ SVAQRAQGKS YVFFDGPPFA TGLPHFGHFV
     PSTIKDIIPR YQTMRGAYVP RRFGWDCHGL PIEHLIEQEL NLNSKSDVES YGVSAFNAAC
     RSSVLRYVKE WQRTLTRLGR WVDFDNDYKT MDVCYMESVW WVVAQLWQRK LLYEGYKILP
     YCPRCATALS NHELNLGGYQ DVSDPAITVR FECTSVVPGS PAAREFCAAA SWGSASLPAH
     TCFLAWTTTP WTLPCNAALA LGPQILYVLI EANDEHYILA RSRLEFYYPD SSAYRVVWEK
     RGEHLAGIRY RPLFSYPVFG QGPDPSVQGD SEEGLFCTRV ADFVSTEDGT GVVHVAPAFG
     EDDYEVFKDA GISIQCPLDA ECRFTAEVAD YQGLFVKAAD KAIIARVQKQ GALFRREQIS
     HAYPHCWRCA SPLIYRAVHS WFVAVEKIKD KMLAANASIC WQPSHIRDGR FGKWLVCARD
     WAISRDRYWG NPLPIWRCVH CGATDCIGSR TQLYERSGML LEDLHKHVVD MVTIPCACGS
     VMRRVPEVLD CWFESGAMPY AQQHYPFEHA TDFERYFPAH FISEGLDQTR GWFYTLTILA
     VALFERPAFE NCIVTGLVLA SDGKKMSKAL RNYADPNEVM DRYGADALRL FLVRSAVVRA
     DDLKYSDEGV KDILKTVIIP LWNSYSFYVT YANIDGIDPP VCAKVDGMGQ AVTRLATHLN
     NPLDRWILSL TEKLVQDIAC ALDAYDVSKV ADPIVSYVDQ LNNWYIRRSR RRFWKSINDE
     DKRCAYNTLY CVLKRCVLAI APVVPFITES IWQNIRAADD VQSVHLADYP VCTPMVRDDA
     LEFKMETVQR VVSMARAIRA QCNLKVRQPL KAMQVITRNP MERSALLEME EDVLDELNVK
     ELVFHEKEDE IVEYRAKANF RVLGKELGSK TKRAALSIER LSSAEIQEIL EGTTLYLDVD
     GDRLELTEEK ILVQRIERES LKAINEGTLT VALDTTLTED LLLEGAIRDL VRGVQNLRKE
     RGFSLVDRIC LRVFSSDQDI VCARKAYDLH RSYIVGETLA AHVQWARVRD GASAVYVKSD
     AVLWEVSIDK A
//