ID   SYI2_BACHK              Reviewed;        1033 AA.
AC   Q6HJF2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Isoleucine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS 2 {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS2 {ECO:0000255|HAMAP-Rule:MF_02003};
GN   OrderedLocusNames=BT9727_1995;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT59742.1; -; Genomic_DNA.
DR   RefSeq; WP_000754926.1; NC_005957.1.
DR   RefSeq; YP_036324.1; NC_005957.1.
DR   AlphaFoldDB; Q6HJF2; -.
DR   SMR; Q6HJF2; -.
DR   EnsemblBacteria; AAT59742; AAT59742; BT9727_1995.
DR   KEGG; btk:BT9727_1995; -.
DR   PATRIC; fig|281309.8.peg.2099; -.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000001301; 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; 2.
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..1033
FT                   /note="Isoleucine--tRNA ligase 2"
FT                   /id="PRO_0000098519"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           590..594
FT                   /note="'KMSKS' region"
FT   BINDING         593
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1033 AA;  118313 MW;  9172970FA3D595E4 CRC64;
     MKKVDVKESA VGRETRIRKQ WNEQSIFEQS IQNREGAQSF VFYEGPPTAN GLPHVGHALG
     RTIKDVVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG ISGKHEIEEY GIEPFTKKCK
     ESVFTYEKQW REFTESIGYW VDMDDPYVTL ENPYIESVWH ILGTIHEKGL LYKGHRVSPY
     CPSCQTSLSS HEVAQGYKTV KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN
     MEYVKAKQEG HVYIVAKERV QDVLKENYEV LSVHKGEELL NTSYTAPFPM KEVTNGYRVI
     GADFVTADSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEVVP FLKGKFVKDC
     DVDIVRYLAK EGLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDTV
     TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE SCDHQFAPKS IADLRKHSTK
     ETPEDLELHK PYVDEVQVSC EKCGSAMNRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE
     QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD
     PVDLVGKFGA DALRWALLVD SAPWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE
     YNPNETYDVK RTKLDEWVLS RLHSTTKKVR TALDDYQFTN AAREIAALVD EVSNWYVRRS
     RNRFWESGMN AEKAAAYETL HDVLVTISKL IAPFTPFVAE DIHLNLTGSS VHLEDYPVVN
     ESLLQPKLEA EMDAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM
     DELNVKAFHV ELDETKYTSY QLKLNFKKAG PKFGKNVNAV NGWLKQLSQD EVQNFVSTER
     AVYEAASGEE VVVTTEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA
     VQEYRKQLNL PVNLRVDVIL DTEEELQQTL TNHKELLEEN LLVKQFTFGH LTNEDDELSL
     GETKVRIKLS AAQ