(data stored in ACNUC7421 zone)

SWISSPROT: TTCA_LEGPC

ID   TTCA_LEGPC              Reviewed;         283 AA.
AC   A5IGL1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 68.
DE   RecName: Full=tRNA-cytidine(32) 2-sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_01850};
DE            EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_01850};
DE   AltName: Full=Two-thiocytidine biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01850};
DE   AltName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000255|HAMAP-Rule:MF_01850};
GN   Name=ttcA {ECO:0000255|HAMAP-Rule:MF_01850}; OrderedLocusNames=LPC_2596;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent 2-thiolation of cytidine in
CC       position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms
CC       are provided by the cysteine/cysteine desulfurase (IscS) system.
CC       {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by
CC       three Cys residues, the fourth Fe has a free coordination site that may
CC       bind a sulfur atom transferred from the persulfide of IscS.
CC       {ECO:0000255|HAMAP-Rule:MF_01850};
CC   -!- PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- MISCELLANEOUS: The thiolation reaction likely consists of two steps: a
CC       first activation step by ATP to form an adenylated intermediate of the
CC       target base of tRNA, and a second nucleophilic substitution step of the
CC       sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S
CC       cluster. {ECO:0000255|HAMAP-Rule:MF_01850}.
CC   -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01850}.
DR   EMBL; CP000675; ABQ56511.1; -; Genomic_DNA.
DR   RefSeq; WP_011945847.1; NC_009494.2.
DR   EnsemblBacteria; ABQ56511; ABQ56511; LPC_2596.
DR   KEGG; lpc:LPC_2596; -.
DR   HOGENOM; HOG000013323; -.
DR   KO; K14058; -.
DR   OMA; IGDEACP; -.
DR   BioCyc; LPNE400673:LPC_RS03945-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01850; TtcA; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012089; tRNA_Cyd_32_2_STrfase.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IGL1.
DR   SWISS-2DPAGE; A5IGL1.
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Magnesium;
KW   Metal-binding; Nucleotide-binding; RNA-binding; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..283
FT                   /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT                   /id="PRO_0000348758"
FT   MOTIF           37..42
FT                   /note="PP-loop motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           112
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           115
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   METAL           203
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ   SEQUENCE   283 AA;  32433 MW;  83AFB9BF25EECE3A CRC64;
     MSSNPSSVEK KLLHYTGKAI ADFNMIRHGD RVMVCLSGGK DSFTLLTILN QLRIKSGNKF
     EIFAFTLDQA QPGWNDACLR QWLAEKSIPH EILTRDTYSI VKEKIPEGKT YCSLCSRLRR
     GIIYRYAEEN GFNKIALGHH RDDLIRTLMM SILYNGDIRS MPPKLLSDNK KHIVIRPLCY
     VQEKDIITFA SEQAFPIIPC NLCGSQENLM RKKVASLIDQ LAIENPKVPS NMLHALQSLK
     PSQLMDQNFW NFKNLEDGLE TAQSVQCEEV FNAQEFEFED EKI
//

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