SYI1_PSEFL
ID SYI1_PSEFL Reviewed; 943 AA.
AC P18330;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Isoleucine--tRNA ligase 1;
DE EC=6.1.1.5;
DE AltName: Full=Isoleucyl-tRNA synthetase 1;
DE Short=IleRS 1;
GN Name=ileS1; Synonyms=ileS;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49323 / NCIMB 10586;
RX PubMed=7929087; DOI=10.1016/s0021-9258(19)51082-1;
RA Yanagisawa T., Lee J.T., Wu H.C., Kawakami M.;
RT "Relationship of protein structure of isoleucyl-tRNA synthetase with
RT pseudomonic acid resistance of Escherichia coli. A proposed mode of action
RT of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase.";
RL J. Biol. Chem. 269:24304-24309(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 701-943.
RC STRAIN=ATCC 49323 / NCIMB 10586;
RX PubMed=2121716; DOI=10.1128/jb.172.11.6512-6517.1990;
RA Isaki L., Beers R., Wu H.C.;
RT "Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II
RT gene (lsp) and flanking genes.";
RL J. Bacteriol. 172:6512-6517(1990).
RN [3]
RP RESISTANCE TO MUPIROCIN.
RC STRAIN=ATCC 49323 / NCIMB 10586;
RX PubMed=12672810; DOI=10.1074/jbc.m302633200;
RA Yanagisawa T., Kawakami M.;
RT "How does Pseudomonas fluorescens avoid suicide from its antibiotic
RT pseudomonic acid? Evidence for two evolutionarily distinct isoleucyl-tRNA
RT synthetases conferring self-defense.";
RL J. Biol. Chem. 278:25887-25894(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) (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Confers resistance to the antibiotic mupirocin (pseudomonic
CC acid A), an Ile-analog produced by P.fluorescens NCIMB 10586 itself
CC that competitively inhibits activation by Ile-tRNA synthetase, thus
CC inhibiting protein biosynthesis.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 -!- MISCELLANEOUS: P.fluorescens NCIMB 10586 possesses two distinct IleRSs
CC (IleRS-R1 and IleRS-R2), each with a different level of sensitivity to
CC mupirocin. Purified IleRs-R2 shows no sensitivity to mupirocin even at
CC a concentration of 5 mM, 100'000 fold higher than the Ki value of
CC IleRS-R1.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000305}.
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DR EMBL; X80132; CAA56431.1; -; Genomic_DNA.
DR EMBL; M35366; AAA25883.1; -; Genomic_DNA.
DR EMBL; M35367; AAA26022.1; ALT_SEQ; Genomic_DNA.
DR PIR; A37152; A37152.
DR AlphaFoldDB; P18330; -.
DR SMR; P18330; -.
DR STRING; 690597.JH730966_gene5350; -.
DR PRIDE; P18330; -.
DR eggNOG; COG0060; Bacteria.
DR SABIO-RK; P18330; -.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
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; Antibiotic resistance; ATP-binding; Cytoplasm;
KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..943
FT /note="Isoleucine--tRNA ligase 1"
FT /id="PRO_0000098445"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 608..612
FT /note="'KMSKS' region"
FT BINDING 567
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000250"
FT BINDING 611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 926
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 929
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 28..29
FT /note="IL -> SC (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 755..756
FT /note="QT -> DR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 758..759
FT /note="LY -> VP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 761..764
FT /note="ISEA -> QRR (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 943 AA; 105719 MW; 6827B2BF2EB89FC0 CRC64;
MTDYKATLNL PDTAFPMKAG LPQREPQILQ RWNSIGLYGK LREIGKDRPK FVLHDGPPYA
NGTIHIGHAL NKILKDMILR SKTLSGFDAP YVPGWDCHGL PIEHKVEVTY GKNLGADKTR
ELCRAYATEQ IEGQKSEFIR LGVLGEWDNP YKTMNFKNEA GEIRALAEIV KGGFVFKGLK
PVNWCFDCGS ALAEAEVEYE DKKSSTIDVA FPIADDAKLA EAFGLASLAK PAAIVIWTTT
PWTIPANQAL NVHPEFTYAL VDVGDRLLVL AEEMVESCLA RYELQGSVIA TATGSALELI
NFRHPFYDRL SPVYLADYVE LGSGTGIVHC SPAYGVDDFV ICKKYGMVND DIINPVQSNG
VYVPSLEFFG GQFIFKADQP IIEKLREVGA LMQTAAIQHS YMHCWRHKTP LIYRATAQWF
IGMDKEPTSG DTLRVRSLKA IEDTKFVPSW GQARLHSMIA NRPDWCISRQ RNWGVPIPFF
LNKESGELHP RTVELMEVVA QRVEQQGIEA WFKLDAAELL GDEAPLYDKI SDTLDVWFDS
GTTHWHVLRG SHPMGHETGP RADLYLEGSD QHRGWFHSSL LTGCAIDNHA PYRELLTHGF
TVDETGRKMS KSLKNVIEPK KINDTLGADI MRLWVASTDY SGEIAVSDQI LARSADAYRR
IRNTARFMLS NLTGFNPASD LLPAEDMLAL DRWAVDRTLL LQRELQEHYG EYRFWNVYSK
IHNFCVQELG GFYLDIIKDR QYTTGANSKA RRSAQTALYH ISEALVRWIA PILAFTADEL
WEYLPGERNE SVMLNTWYEG LTELPADFEL GREYWEGVMA VKVAVNKELE VQRAAKAVGG
NLQAEVTLFA EDGLTADLAK LSNELRFVLI TSTASLAPFT QAPADAVATE VPGLKLKVVK
SAFPKCARCW HCREDVGVNP EHPEICGRCV DNISGEGEVR HYA
