ID   SYI2_BACCZ              Reviewed;        1033 AA.
AC   Q63BZ8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=BCE33L1977;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
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; CP000001; AAU18279.1; -; Genomic_DNA.
DR   RefSeq; WP_000754914.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q63BZ8; -.
DR   SMR; Q63BZ8; -.
DR   EnsemblBacteria; AAU18279; AAU18279; BCE33L1977.
DR   KEGG; bcz:BCE33L1977; -.
DR   PATRIC; fig|288681.22.peg.3547; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000002612; 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_0000098518"
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;  118486 MW;  2AE9F189D2EBC158 CRC64;
     MKKVDVKESA VGRETRIRKQ WNEQSIFEQS IQNREGAQSF VFYEGPPTAN GLPHVGHALG
     RTIKDVVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG ISGKHEIEEY GIEPFIKKCK
     ESVFTYEKQW REFTESIGYW VDMDDPYVTL ENPYIESVWH ILGTIHEKGL LYKGHRVSPY
     CPSCQTSLSS HEVAQGYKTV KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN
     MEYVKAKQEG HVYIVAKERV QDVLKENYEV LSVHKGEELL NISYTAPFPM KEVTNGYRVI
     GADFVTADSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEAVP FLKGKFVKDC
     DVDIVRYLAK EGLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDSV
     TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE SCDHQFAPKS IDDLRKHSTK
     ETQEDLELHK PYVDEVQVCC EKCGGTMTRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE
     QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD
     PVDLVNQFGA DALRWALLVD SAPWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE
     YNPNETYDVK RTKLDEWVLS RLHSTTKKVR IALDDYQFTN AAREIAALVD EVSNWYVRRS
     RNRFWESGMN AEKAAAYETL HDVLVTISKL IAPFTPFVAE DIHLNLTGSS VHLEDYPVVN
     ESLLQPKLEA EMNAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM
     DELNVKAFHV ELDETKYTSY QLKLNFKTAG PKFGKNVNAV NGWLKQLSQD EVQNFVSTER
     AVYEVASGEE IVVTTEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA
     VQEYRKQLNL PVNLRVDVIL DTEEELQQTL TNHKELLEEN LLVKQFTFGH LTNEDDELSL
     GETKVRIKLS ATK