TTCA_PSE14
ID TTCA_PSE14 Reviewed; 274 AA.
AC Q48FG8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=PSPPH_3726;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-
CC [cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP +
CC diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase];
CC Xref=Rhea:RHEA:57048, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:12157,
CC Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:14821, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:82748, ChEBI:CHEBI:141453, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01850};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57049;
CC Evidence={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}.
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DR EMBL; CP000058; AAZ37004.1; -; Genomic_DNA.
DR RefSeq; WP_002554625.1; NC_005773.3.
DR AlphaFoldDB; Q48FG8; -.
DR SMR; Q48FG8; -.
DR STRING; 264730.PSPPH_3726; -.
DR EnsemblBacteria; AAZ37004; AAZ37004; PSPPH_3726.
DR GeneID; 61871205; -.
DR KEGG; psp:PSPPH_3726; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_026481_0_0_6; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 1051352at2; -.
DR Proteomes; UP000000551; Chromosome.
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;
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..274
FT /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT /id="PRO_0000348803"
FT MOTIF 40..45
FT /note="PP-loop motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 206
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ SEQUENCE 274 AA; 31127 MW; A4EF6503DD93EA1C CRC64;
MGTLSVNQNK LQKRLRRLAG EAVADFNMIE EGDKVMVCLS GGKDSYTMLD VLMHLQKVAP
IKFDIVAVNM DQKQPGFPEH VLPAYLKELG IEYHIVEKDT YSVVKELIPE GKTTCSLCSR
LRRGTLYTFA DEIGATKMAL GHHRDDIVET FFLNMFFNGS LKAMPPKLRA DDGRNVVIRP
LAYCHEKDIQ AYSDLKQFPI IPCNLCGSQE NLQRQVVKDM LIDWERKTPG RTESIFRALQ
NVQPSQLADR NLFDFSNLRI DETAASRFVN VVNI
