ID   SYI_STAEQ               Reviewed;         916 AA.
AC   Q5HPZ9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Isoleucine--tRNA ligase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   Name=ileS; OrderedLocusNames=SERP0758;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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) (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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)) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 1 subfamily. {ECO:0000305}.
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DR   EMBL; CP000029; AAW54153.1; -; Genomic_DNA.
DR   RefSeq; WP_002490488.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPZ9; -.
DR   SMR; Q5HPZ9; -.
DR   STRING; 176279.SERP0758; -.
DR   PRIDE; Q5HPZ9; -.
DR   EnsemblBacteria; AAW54153; AAW54153; SERP0758.
DR   KEGG; ser:SERP0758; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_7_1_9; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000531; 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; 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   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 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; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..916
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098472"
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:0000250"
FT   BINDING         598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         888
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         905
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         908
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   916 AA;  105164 MW;  E2703272E7420212 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 QWFASINKVR
     QDILDAIEDT NFKVDWGKTR IYNMIRDRGE WVISRQRVWG VPLPVFYAEN GDIIMTKETV
     NHVADLFEKH GSNIWFEKEA KELLPEGFSH PGSPNGEFTK ETDIMDVWFD SGSSHRGVLE
     TRPELSFPAD LYFEGSDQYR GWFNSSITTA VATRGQAPYK FLLSHGFVMD GEGKKMSKSL
     GNVIVPDQVV KQKGADIARL WVSSTDYLSD VRISDEILKQ TSDVYRKIRN TLRFMLGNIN
     DFNPETDSIA ETNLLEVDRY LLNRLREFTA STINNYENFD YLNIYQEVQN FINVELSNFY
     LDYGKDILYI EKKDSHKRRS MQTVLYQILV DMTKLLAPIL VHTAEEVWSH TPHVKEESVH
     LSDMPKVVDV DEELLEKWNT FMNLRDDVNR ALEQARNEKV IGKSLEAKVV IGSNESFNTA
     EFLQQFNDLQ QLFIVSQVEV KDKVNDGVSY QYGDIHIKHA EGEKCERCWN YTEELGSVGE
     LEHLCPRCQE VVKTLV