ID   SYI2_BACCR              Reviewed;        1033 AA.
AC   Q81E30;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 121.
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=BC_2164;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP09130.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016877; AAP09130.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_831929.1; NC_004722.1.
DR   RefSeq; WP_000416534.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81E30; -.
DR   SMR; Q81E30; -.
DR   STRING; 226900.BC_2164; -.
DR   EnsemblBacteria; AAP09130; AAP09130; BC_2164.
DR   KEGG; bce:BC2164; -.
DR   PATRIC; fig|226900.8.peg.2186; -.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000001417; 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; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Zinc.
FT   CHAIN           1..1033
FT                   /note="Isoleucine--tRNA ligase 2"
FT                   /id="PRO_0000098517"
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;  118308 MW;  3BDB95615706F6A2 CRC64;
     MEKVDVKESA VGREMRIRKQ WNEQNIFEQS IQNREGAQSF VFYEGPPTAN GLPHVGHALG
     RTIKDLVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG ISGKHEIEEY GIEPFIQKCK
     ESVFTYEKQW REFTESIGYW VDMDDPYVTL KNPYIESVWH ILGTIHEKGL LYKGHRVSPY
     CPSCQTSLSS HEVAQGYKTV KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN
     MEYVKAKQES HVYIVAKERV QEVLKENYEV LSVHKGEELL NTSYTAPFPM KEVTNGYRVI
     AADFVTGDSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEAVP FLKGKFVKDC
     DVDIVRYLAK EGLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDSV
     TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE SCDHQFAPKS IAELRKHSTK
     ETPEDLELHK PYVDEVQVCC GKCGGTMNRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE
     QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD
     PVDLVDKFGA DALRWALLVD SAPWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE
     YNPKETYDVK LTKLDEWVLS RLHSTTKKVR TALDDYQFTN AAREIAALVD EVSNWYVRRS
     RNRFWESGMN AEKAAAYETL HEVLVTISKL IAPFTPFVAE DIHLNLEGSS VHLADYPVVN
     ESLLQPKLEA EMDAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM
     DELNVKAFHV ELDETKYTSY QLKLNFKTAG PKFGKNVNAV NGWLKQLSQE EVQNFVSTGR
     AVYEATPEGE VVVTGEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA
     VQEYRKQLNL PVNLRVDIIL DTEEELQRTL TNHKDLLEEN LLVKQFTFGH LTNEDDELSL
     GETKLRIKLS AAN