SYI2_BACAN
ID SYI2_BACAN Reviewed; 1033 AA.
AC Q81R75; Q6HZE8; Q6KTD8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=BA_2181, GBAA_2181, BAS2027;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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_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; AE016879; AAP26060.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT31298.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT54341.1; -; Genomic_DNA.
DR RefSeq; NP_844574.1; NC_003997.3.
DR RefSeq; WP_000754882.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_028290.1; NC_005945.1.
DR AlphaFoldDB; Q81R75; -.
DR SMR; Q81R75; -.
DR IntAct; Q81R75; 1.
DR STRING; 260799.BAS2027; -.
DR DNASU; 1085720; -.
DR EnsemblBacteria; AAP26060; AAP26060; BA_2181.
DR EnsemblBacteria; AAT31298; AAT31298; GBAA_2181.
DR GeneID; 45022084; -.
DR KEGG; ban:BA_2181; -.
DR KEGG; bar:GBAA_2181; -.
DR KEGG; bat:BAS2027; -.
DR PATRIC; fig|198094.11.peg.2150; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_9; -.
DR OMA; KMMAPFT; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; Reference proteome; Zinc.
FT CHAIN 1..1033
FT /note="Isoleucine--tRNA ligase 2"
FT /id="PRO_0000098515"
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; 118653 MW; 4E393F801CC74A8B CRC64;
MKKVDVKESA VGREMRIRKQ WNEQNIFEQS 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 EDLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDTV
TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE RCDHQFAPKS IADLRKHSMK
ETPEDLELHK PYVDEVQVCC EKCGSTMNRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE
QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD
PVDLVGKFGA DALRWALLVD SALWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE
YNPNETYDVK RTKLDEWVLS RLHSTTKKVR TALDDYQFTN AAREIAALVD EVSNWYVRRS
RNRFWESGMN AEKAAAYETL HDVLVTISKL IAPFTPFVAE DVHLNLTGSS VHLEDYPVVN
ESLLQPKLEA EMDAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM
DELNVKAFHV ELDETKYTSY QLKLNFKKAG PKFGKNVNAV NGWLKQLSQD EVQNFVSTER
AVYEVAPGEE IVVTTEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA
VQEYRKQLNL PVNLRVDVIL DTEEELQQTL TNHKELLEEN LLVKQFTFGH LTNEDDELSL
GETKVRIKLS TAQ
