ID   SYI_BACSU               Reviewed;         921 AA.
AC   Q45477; O31730; P71022;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002};
GN   OrderedLocusNames=BSU15430;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   SEQUENCE REVISION TO 744.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RC   STRAIN=168;
RA   Stewart G.C., Cha J.H.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 733-921.
RC   STRAIN=168;
RA   Pragai Z., Tjalsma H., Bolhuis A., van Dijl J.M., Venema G., Bron S.;
RL   Submitted (FEB-1996) 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_02002}.
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_02002};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR   EMBL; AL009126; CAB13417.2; -; Genomic_DNA.
DR   EMBL; U60901; AAB49280.1; -; Genomic_DNA.
DR   EMBL; U48870; AAB57764.1; -; Genomic_DNA.
DR   PIR; H69643; H69643.
DR   RefSeq; NP_389426.2; NC_000964.3.
DR   RefSeq; WP_003245512.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; Q45477; -.
DR   SMR; Q45477; -.
DR   IntAct; Q45477; 1.
DR   MINT; Q45477; -.
DR   STRING; 224308.BSU15430; -.
DR   jPOST; Q45477; -.
DR   PaxDb; 224308-BSU15430; -.
DR   EnsemblBacteria; CAB13417; CAB13417; BSU_15430.
DR   GeneID; 940119; -.
DR   KEGG; bsu:BSU15430; -.
DR   PATRIC; fig|224308.179.peg.1682; -.
DR   eggNOG; COG0060; Bacteria.
DR   InParanoid; Q45477; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q45477; -.
DR   BioCyc; BSUB:BSU15430-MONOMER; -.
DR   BRENDA; 6.1.1.5; 658.
DR   SABIO-RK; Q45477; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
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; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..921
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098351"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           594..598
FT                   /note="'KMSKS' region"
FT   BINDING         553
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   921 AA;  104845 MW;  F41081EA48E317E9 CRC64;
     MDFKDTLLMP KTDFPMRGNL PNREPDIQKK WEEEDIYRLV QERTKDRPKF VLHDGPPYAN
     GDIHMGHALN KILKDFIVRY KSMSGYNAPY VPGWDTHGLP IETALTKNKK VNRKEMSVAE
     FRKLCEEYAW KQIEGQREQF KRLGVRGDWE NPYVTLKPEY EAQQIRVFGE MAKRGYIYKG
     LKPVNWSPSS ESALAEAEIE YQDKRSASIY VAFGVKDGKG VLENGERIII WTTTPWTIPA
     NLGISVHPDL EYSVIAVGED RFVVASALVE NVASACGFDQ YEVTRTVKGK DLENIIAEHP
     LYGRDSLVML GEHVTTDAGT GCVHTAPGHG EDDFIIGQKY GLDVLCPVDE KGVMTSEAPG
     FEGMFYDDAN KAITQQLDEK GALVKLEFIT HSYPHDWRTK KPTIFRATAQ WFASIKDFRS
     DLLDAIKETK WVPEWGEQRL HNMVRDRGDW CISRQRAWGV PIPVFYAENG EPVITDETIE
     HVSELFRQHG SNIWFEKEAK DLLPEGFTHP GSPNGTFTKE QDIMDVWFDS GSSHQAVLEE
     RDDLVRPADL YLEGSDQYRG WFNSSLSTAV AVTGKAPYKG VLSHGFALDG EGRKMSKSIG
     NVVVPAKVMK QLGADILRLW VSSVDYQADV RVSDAILKQV AEVYRKIRNT FRFLHGNLFD
     FDPKTNAVAV EDLREVDQYM LIKLNKLIDK VKKAYDEYEF AVVYHSIHNF CTIELSSFYL
     DFAKDIVYIE HADHPDRRSM QTVFYETLLA LVKLSAPILP HTADELWSHL TFVEEQSVQL
     TDMPETITVP NSEATEEKFD RFMALRDDVL KALETARNEK IIGKSLEANL KLYPNKENKE
     LLASIKENLS QLFIVSELTI SEENEAPNDA QSFATGKIAV EKAEGEMCER SRVISKDVGA
     NPKYPTLSLR NAEIVEKYYQ K
//