TTCA_SORC5
ID TTCA_SORC5 Reviewed; 283 AA.
AC A9G6U6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, 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=sce2581;
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56;
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN92740.1; -; Genomic_DNA.
DR RefSeq; WP_012235213.1; NC_010162.1.
DR AlphaFoldDB; A9G6U6; -.
DR SMR; A9G6U6; -.
DR STRING; 448385.sce2581; -.
DR EnsemblBacteria; CAN92740; CAN92740; sce2581.
DR KEGG; scl:sce2581; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_026481_0_0_7; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 1051352at2; -.
DR BioCyc; SCEL448385:SCE_RS13220-MON; -.
DR Proteomes; UP000002139; 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..283
FT /note="tRNA-cytidine(32) 2-sulfurtransferase"
FT /id="PRO_0000348858"
FT MOTIF 32..37
FT /note="PP-loop motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01850"
SQ SEQUENCE 283 AA; 30982 MW; 16D1AF04294A72BC CRC64;
MQLRRKLARA MGRAITDFDM IADGDRILCA VSGGKDSYAM HALLVDLARR APVRFSVIAV
NIDQGHPGYP GHLLTDYMAA GGHEFRMISE DTYSIVTEKI PENKTYCSLC SRLRRGILYR
IARELGCSKI ALGHHRDDAV TTLLLNLIFA GQLKSMPPKL ISDDGDNIVI RPLIYCAEAE
LAAFAAEERF PIIPCDLCGS QENLQRKAVS QLLADLDARH PGTRQNMLAA LGNVRPSHLF
DTGLWKRLGL EVAREEGSAR DEAGVGAPAP DVLPVGNLLR NLA
