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Database: UniProt
Entry: M5J5N3_9LACO
LinkDB: M5J5N3_9LACO
Original site: M5J5N3_9LACO 
ID   M5J5N3_9LACO            Unreviewed;       449 AA.
AC   M5J5N3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161};
GN   ORFNames=D271_07369 {ECO:0000313|EMBL:EKW98350.1};
OS   Ligilactobacillus saerimneri 30a.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW98350.1, ECO:0000313|Proteomes:UP000011912};
RN   [1] {ECO:0000313|EMBL:EKW98350.1, ECO:0000313|Proteomes:UP000011912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30a {ECO:0000313|EMBL:EKW98350.1,
RC   ECO:0000313|Proteomes:UP000011912};
RX   PubMed=23405290;
RA   Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA   Lolkema J.S., Lucas P.M.;
RT   "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT   sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT   Biogenic Amines.";
RL   Genome Announc. 1:E00097-E00012(2013).
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000047, ECO:0000256|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKW98350.1}.
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DR   EMBL; ANAG01000022; EKW98350.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5J5N3; -.
DR   STRING; 1227363.D271_07369; -.
DR   PATRIC; fig|1227363.6.peg.1445; -.
DR   Proteomes; UP000011912; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; HUPs; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR012796; Lysidine-tRNA-synth_C.
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   NCBIfam; TIGR02433; lysidine_TilS_C; 1.
DR   NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR   PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43033:SF1; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011912};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          373..445
FT                   /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00977"
SQ   SEQUENCE   449 AA;  52639 MW;  6AAF2F319562A623 CRC64;
     MDLEKQFYQR IQNLGLARKK VLVAYSTGVD STVLLHLLQT LPVAVRPQIY VAYIDHQIRE
     QSVVETAYVK EYCRRQHLPL FVKVWPRADH PATGVEAAGR EIRYHFFAET MQREGIPYLV
     TAHHANDQAE TFLMKLLRGG DLEQLVGIRH QRQFQGKFRL VRPLLGISKA TLRHYATVHQ
     LKYFEDYTNH TDDYLRNRMR HNVVPRLQAE NEQTLAHIQE YQDQLADVLM VAQAAAAAKL
     DEIKLRTGRY LVAYWVRLAS PWKKLVLKEL CRTQHVQITG EQLEQCVALL RNDSKPQGQV
     MLGQSWWLVK EYTVFYLAQR ADNHVDSDEK YELKLNQWVN ISAYERFGLF EVTTYQPELH
     DDVLKIDSLD KPLYIRHRRP HDRLKTTSGS QKVKRILIDH KIPRSQRDQI WLVTTDENEV
     LWVVGLKKSD LSRPADHAKI QYVIVHQSR
//
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