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   16-JUN-2009, entry version 69.
DE   RecName: Full=Isoleucyl-tRNA synthetase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucine--tRNA ligase;
DE            Short=IleRS;
GN   Name=ileS; OrderedLocusNames=BSU15430;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 0:0-0(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
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)) (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily.
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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_389426.1; -.
DR   HSSP; P41972; 1QU3.
DR   GeneID; 940119; -.
DR   GenomeReviews; AL009126_GR; BSU15430.
DR   KEGG; bsu:BSU15430; -.
DR   NMPDR; fig|224308.1.peg.1545; -.
DR   SubtiList; BG11792; ileS.
DR   HOGENOM; Q45477; -.
DR   OMA; Q45477; FPMRGNL.
DR   BioCyc; BSUB224308:BSU1545-MON; -.
DR   BRENDA; 6.1.1.5; 150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02002; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR010663; DNA_glyclase/IsotRNA_synth_Znf.
DR   InterPro; IPR002301; Ile-tRNA-synt_Ia.
DR   InterPro; IPR015905; Ile-tRNA-synt_Ia_N.
DR   InterPro; IPR018353; Isoleucyl-tRNA_synthetase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF9; Ile-tRNA-synt_Ia; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    921       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_0000098351.
FT   MOTIF        57     67       "HIGH" region.
FT   MOTIF       594    598       "KMSKS" region.
FT   BINDING     553    553       Aminoacyl-adenylate (By similarity).
FT   BINDING     597    597       ATP (By similarity).
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
//