TTUC_THET2
ID TTUC_THET2 Reviewed; 271 AA.
AC Q72J02;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sulfur carrier protein adenylyltransferase {ECO:0000305|PubMed:19037260};
DE AltName: Full=E1-like protein TtuC {ECO:0000303|PubMed:22467871};
DE AltName: Full=Sulfur carrier protein MoaD adenylyltransferase {ECO:0000305|PubMed:19037260};
DE EC=2.7.7.80 {ECO:0000269|PubMed:19037260};
DE AltName: Full=Sulfur carrier protein ThiS adenylyltransferase {ECO:0000305|PubMed:19037260};
DE EC=2.7.7.73 {ECO:0000269|PubMed:19037260};
DE AltName: Full=Sulfur carrier protein TtuB adenylyltransferase {ECO:0000305|PubMed:19037260};
DE EC=2.7.7.- {ECO:0000269|PubMed:19037260};
DE AltName: Full=tRNA two-thiouridine-synthesizing protein C {ECO:0000303|PubMed:19037260};
GN Name=ttuC {ECO:0000303|PubMed:19037260};
GN Synonyms=moeB {ECO:0000312|EMBL:AAS81321.1};
GN OrderedLocusNames=TT_C0979 {ECO:0000312|EMBL:AAS81321.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, CROSS-LINKING
RP TO SULFUR CARRIER PROTEIN TTUB, AND MUTAGENESIS OF CYS-192 AND CYS-268.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=19037260; DOI=10.1038/emboj.2008.246;
RA Shigi N., Sakaguchi Y., Asai S., Suzuki T., Watanabe K.;
RT "Common thiolation mechanism in the biosynthesis of tRNA thiouridine and
RT sulphur-containing cofactors.";
RL EMBO J. 27:3267-3278(2008).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, CONJUGATION TO TTUB, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=22467871; DOI=10.1074/jbc.m112.359844;
RA Shigi N.;
RT "Posttranslational modification of cellular proteins by a ubiquitin-like
RT protein in bacteria.";
RL J. Biol. Chem. 287:17568-17577(2012).
CC -!- FUNCTION: Adenylyltransferase involved in the biosynthesis of several
CC sulfur compounds. Is required for the 2-thiolation of 5-methyluridine
CC residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-
CC thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal
CC stabilization of tRNAs in thermophilic microorganisms, and is essential
CC for cell growth at high temperatures. TtuC catalyzes the adenylation by
CC ATP of the carboxyl group of the C-terminal glycine of sulfur carrier
CC protein TtuB. Is also involved in the biosynthesis of thiamine,
CC molybdenum cofactor (Moco) and probably tungsten cofactor (Wco), by
CC adenylating the sulfur carriers ThiS and MoaD (PubMed:19037260). Is
CC required for the conjugation of TtuB to target proteins
CC (PubMed:22467871). {ECO:0000269|PubMed:19037260,
CC ECO:0000269|PubMed:22467871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC ChEBI:CHEBI:90778; EC=2.7.7.80;
CC Evidence={ECO:0000269|PubMed:19037260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly + ATP + H(+)
CC = [sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + diphosphate;
CC Xref=Rhea:RHEA:43344, Rhea:RHEA-COMP:12909, Rhea:RHEA-COMP:12910,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.73;
CC Evidence={ECO:0000269|PubMed:19037260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[TtuB sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+)
CC = [TtuB sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate;
CC Xref=Rhea:RHEA:55168, Rhea:RHEA-COMP:13342, Rhea:RHEA-COMP:14113,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:90618, ChEBI:CHEBI:90778;
CC Evidence={ECO:0000269|PubMed:19037260};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P30138};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P30138};
CC -!- ACTIVITY REGULATION: Enzymatic activity may be regulated by TtuB
CC conjugation. {ECO:0000305|PubMed:22467871}.
CC -!- PATHWAY: tRNA modification. {ECO:0000269|PubMed:19037260}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000269|PubMed:19037260}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000269|PubMed:19037260}.
CC -!- PTM: Conjugated to TtuB via a covalent linkage that likely involves a
CC lysine residue (PubMed:22467871). Is able to form a covalent thioester
CC adduct with TtuB via Cys-192 in vitro (PubMed:19037260).
CC {ECO:0000269|PubMed:19037260, ECO:0000269|PubMed:22467871}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene completely abolishes the
CC presence of m(5)s(2)U in tRNAs, although its precursor, 5-methyluridine
CC (ribothymidine) is present; other nucleoside modifications remain
CC unchanged (PubMed:19037260). These deletion mutants exhibit a
CC temperature-sensitive phenotype similar to the ttuA and ttuB deletion
CC mutants, they are unable to grow above 80 degrees Celsius
CC (PubMed:19037260). They are also unable to synthesize thiamine and
CC molybdenum cofactor (PubMed:19037260). No TtuB-protein conjugate is
CC formed and only free TtuB is detected in the ttuC deletion strain
CC (PubMed:22467871). {ECO:0000269|PubMed:19037260,
CC ECO:0000269|PubMed:22467871}.
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR EMBL; AE017221; AAS81321.1; -; Genomic_DNA.
DR RefSeq; WP_011173400.1; NC_005835.1.
DR AlphaFoldDB; Q72J02; -.
DR SMR; Q72J02; -.
DR STRING; 262724.TT_C0979; -.
DR EnsemblBacteria; AAS81321; AAS81321; TT_C0979.
DR KEGG; tth:TT_C0979; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_10_0_0; -.
DR OMA; MIYDALE; -.
DR OrthoDB; 1408716at2; -.
DR UniPathway; UPA00060; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isopeptide bond; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW Nucleotidyltransferase; Thiamine biosynthesis; Thioester bond; Transferase;
KW tRNA processing; Ubl conjugation; Zinc.
FT CHAIN 1..271
FT /note="Sulfur carrier protein adenylyltransferase"
FT /id="PRO_0000442737"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 129..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30138"
FT CROSSLNK 192
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in TtuB)"
FT /evidence="ECO:0000269|PubMed:19037260"
FT MUTAGEN 192
FT /note="C->S: Not able to form a thioester complex with
FT TtuB."
FT /evidence="ECO:0000269|PubMed:19037260"
FT MUTAGEN 268
FT /note="C->S: Still able to form a thioester complex with
FT TtuB."
FT /evidence="ECO:0000269|PubMed:19037260"
SQ SEQUENCE 271 AA; 29628 MW; 8CCADEBA2F574B0F CRC64;
MRWTKEELDR YHRQMILPQV GPEGQERLKR ASVVVVGAGG LGVPVLQYLV AAGVGRVGVV
EMDRVEVSNL HRQVLYTTED VGEPKALVAQ KRLQALNPLV RVEAYPVRLT SENALEILRP
YDLVVDASDN FPTRYLVNDA AVLLGKPLVF GAIYQFDGQV AVFHHPTLHG EMGPCYRCLF
PKPPPPGAVP SCAEAGVFGV LPAVVGSLMA AEALKVLLGI GKPLAGHLLL YDALEASFRK
LTVRRNPRCP VCGDEPTQRE LVDYEAFCGL R
