ID   TILS_PSYWF              Reviewed;         525 AA.
AC   A5WCA0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161};
GN   OrderedLocusNames=PsycPRwf_0336;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine.
CC       {ECO:0000255|HAMAP-Rule:MF_01161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}.
CC   -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC       motif, predicted to be a P-loop motif involved in ATP binding.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01161}.
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DR   EMBL; CP000713; ABQ93291.1; -; Genomic_DNA.
DR   RefSeq; WP_011959625.1; NC_009524.1.
DR   AlphaFoldDB; A5WCA0; -.
DR   SMR; A5WCA0; -.
DR   STRING; 349106.PsycPRwf_0336; -.
DR   EnsemblBacteria; ABQ93291; ABQ93291; PsycPRwf_0336.
DR   KEGG; prw:PsycPRwf_0336; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_018869_2_0_6; -.
DR   OMA; WLACSGG; -.
DR   OrthoDB; 666797at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
DR   PANTHER; PTHR43033; PTHR43033; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF09179; TilS; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT   CHAIN           1..525
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_1000073075"
FT   BINDING         32..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   525 AA;  59124 MW;  27472BC703849666 CRC64;
     MTTPVCISQA FMDSFHAHHA QLLGKRVWLA CSGGRDSLGL ALLCRTLFDQ GRLPFLPQLI
     HVNHGMQAAN DEWAQQVAQW AQQHDMACQI IGLNLTHKSE QAARDGRYQA MMQLMNQDDV
     LILGHHQDDQ VETLLMRLFN GAGVTGLGAM REWTSKQAHT AQSPPDVNKP RQRIFLWRPW
     LEISRDQITE YAQRHNLKYI DDPTNVAQSP SKLALQTLND RAWLRSVLLP HITERYPQAS
     EAMARTAQLM QQASDSIDEQ VTQDLAQVAL AATEQQSVIA LDKLAGLSAP RQAALIHHWL
     APYPNQLPPS KRLVDEVLAL SFRQDSNHQT CLYFDAGSEQ YQVRRYQNKL YRLQHAYAQW
     LQMMPHQIHL PLAHNAEELS LNLADTDVLS LKQSGLEFDW QLTGVRGLMA HLARLLNSAD
     AKVTPCQLIF EPLPRTIKLA LAGRSGRKSG KKLLQALDQP SFMRGSVVLC RLDMMGSDGI
     LQDSSTAVPL FIICIDRIWV LQSQFTALIN QLLATEVLST QILEC