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TTCA_CITBB
ID   TTCA_CITBB              Reviewed;         255 AA.
AC   B5ED57;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Gbem_0615;
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) 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   -!- 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; CP001124; ACH37643.1; -; Genomic_DNA.
DR   RefSeq; WP_012529050.1; NC_011146.1.
DR   AlphaFoldDB; B5ED57; -.
DR   SMR; B5ED57; -.
DR   STRING; 404380.Gbem_0615; -.
DR   EnsemblBacteria; ACH37643; ACH37643; Gbem_0615.
DR   KEGG; gbm:Gbem_0615; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_026481_0_0_7; -.
DR   OMA; MNLDQKQ; -.
DR   OrthoDB; 1051352at2; -.
DR   Proteomes; UP000008825; 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; Reference proteome; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..255
FT                   /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT                   /id="PRO_1000188644"
FT   MOTIF           37..42
FT                   /note="PP-loop motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
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         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ   SEQUENCE   255 AA;  28944 MW;  BE16159D3394BB9D CRC64;
     MALIEDAAFT RIKNRVGKAI AEFDLISEGD RVAVAVSGGK DSYTMLHMLE TLRRRAPVRY
     ELVAINIDSG YRGYRADIIE EHLREHGFTY HMEKTDHYDI ISEKRRPNSS YCSICARLKR
     GTLYTLAQQY GCNKLALGHH MDDFIETLLL NQFFVGSLKA MAPSMLADNG VTTVIRPLVY
     VPEKEIIPFS RNNRFPVVCC CCPVCGTADL QRKKMKELLE TLERDNPLVK KSLLTALSNV
     HPRHLLDKGL TRKPS
 
 
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