SYI_STAEP
ID SYI_STAEP Reviewed; 871 AA.
AC Q846V6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002};
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12615863; DOI=10.1093/jac/dkg140;
RA Yun H.J., Lee S.W., Yoon G.M., Kim S.Y., Choi S., Lee Y.S., Choi E.C.,
RA Kim S.;
RT "Prevalence and mechanisms of low- and high-level mupirocin resistance in
RT staphylococci isolated from a Korean hospital.";
RL J. Antimicrob. Chemother. 51:619-623(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_02002}.
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_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR EMBL; AF516209; AAO65848.1; -; Genomic_DNA.
DR AlphaFoldDB; Q846V6; -.
DR SMR; Q846V6; -.
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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
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;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..871
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098470"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 595..599
FT /note="'KMSKS' region"
FT BINDING 554
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 871 AA; 100134 MW; 2E140C3F74318A15 CRC64;
MNYKDTLLMP KTDFPMRGGL PNKEPQIQEM WDNDDQYRKA LEKNKNNPSF ILHDGPPYAN
GNLHMGHALN KIIKDFIVRY KTMQGFYAPY VPGWDTHGLP IEQALTKKGV DRKKMSVAEF
REKCKEFALK QIDIQKKDFK RLGVRGDFNN PYITLTPEYE AAQIRLFGEM ADKGLIYKGK
KPVYWSPSSE SSLAEAEIEY HDKRSASIYV AFDVKDSKGK VDSDAQFIIW TTTPWTIPSN
VAITVHPELK YGQYNVDGHK YIVAQALSEE VAEALGWDKD SIQLEKEFTG KELEFVEAQH
PFLDRVSLVI NGEHVTTDAG TGCVHTAPGH GEDDYIVGQK YDLPVISPLN DKGVFTEEGG
PFEGMFYDKA NKAVTDLLKE KDALLKLDFI THSYPHDWRT KKPVIFRATP QWFASINKVK
QDILDAIEDT NFKVDWGKTR IYNMIRDRGE WVISRQRVWG VPLPVFYAEN GDIIMTKETV
NHVADLFEKY GSNIWFEKEA KELLPEGFSH PGSPNGEFTK ETDIMDVWFD SGSSHRGVLE
TRPELSFPAD LYFEGSDQYR GWFNSSITTA VATRGQAPYK FLLSHGFVMD GEGKKMSKSL
GNVIVPDQVV KQKGADIARL WVSSTDYLSD VRISDEILKK TSDVYRKIRN TLRFMLGNIN
DFNPETDSIA ETNLLEVDRY LLNRLREFTA STINNYENFD YLNIYQEVQN FINVELSNFY
LDYGKDILYI EKKDSHKRRS MQTVLYQILI DMTKLLAPIL VHTAEEVWSH TPHVKEESVH
LSDMPKVVDV DEELLEKWNT FMNLRDDVNR ALEQARNEKV IGKSLEAKVV IGNNETFNTA
EFLQQFNDLQ QLFIVSQVEV KDKVKLKILI R
