TUSA_ECO57
ID TUSA_ECO57 Reviewed; 81 AA.
AC P0A892; P37618;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Sulfur carrier protein TusA {ECO:0000255|HAMAP-Rule:MF_00413};
DE AltName: Full=Sulfur mediator TusA {ECO:0000255|HAMAP-Rule:MF_00413};
DE AltName: Full=Sulfur transfer protein TusA {ECO:0000255|HAMAP-Rule:MF_00413};
DE AltName: Full=tRNA 2-thiouridine synthesizing protein A {ECO:0000255|HAMAP-Rule:MF_00413};
GN Name=tusA {ECO:0000255|HAMAP-Rule:MF_00413};
GN OrderedLocusNames=Z4844, ECs4319;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) IN COMPLEX WITH ISCS, FUNCTION,
RP INTERACTION WITH ISCS, SUBUNIT, AND MUTAGENESIS OF GLU-21; MET-24;
RP 27-ARG--PRO-35; ARG-27; ARG-31; ASP-45; ARG-50; ASP-51 AND PHE-58.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=20404999; DOI=10.1371/journal.pbio.1000354;
RA Shi R., Proteau A., Villarroya M., Moukadiri I., Zhang L., Trempe J.F.,
RA Matte A., Armengod M.E., Cygler M.;
RT "Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by
RT IscS protein-protein interactions.";
RL PLoS Biol. 8:E1000354-E1000354(2010).
CC -!- FUNCTION: Sulfur carrier protein involved in sulfur trafficking in the
CC cell. Part of a sulfur-relay system required for 2-thiolation during
CC synthesis of 2-thiouridine of the modified wobble base 5-
CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with
CC IscS and stimulates its cysteine desulfurase activity. Accepts an
CC activated sulfur from IscS, which is then transferred to TusD, and thus
CC determines the direction of sulfur flow from IscS to 2-thiouridine
CC formation. Also appears to be involved in sulfur transfer for the
CC biosynthesis of molybdopterin. {ECO:0000255|HAMAP-Rule:MF_00413,
CC ECO:0000305|PubMed:20404999}.
CC -!- PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_00413}.
CC -!- SUBUNIT: Forms a heterotetramer with IscS. Certain pairs of proteins
CC can bind simultaneously to IscS but TusA does not seem to be one of
CC them. IscU can displace TusA from IscS. {ECO:0000269|PubMed:20404999}.
CC -!- INTERACTION:
CC P0A892; P0A6B9: iscS; NbExp=5; IntAct=EBI-15849930, EBI-9011195;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00413}.
CC -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC {ECO:0000255|HAMAP-Rule:MF_00413}.
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DR EMBL; AE005174; AAG58579.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37742.1; -; Genomic_DNA.
DR PIR; G86014; G86014.
DR PIR; G91168; G91168.
DR RefSeq; NP_312346.1; NC_002695.1.
DR RefSeq; WP_000130621.1; NZ_SWKA01000005.1.
DR PDB; 3LVJ; X-ray; 2.44 A; C/D=2-81.
DR PDB; 3LVK; X-ray; 2.44 A; B=2-81.
DR PDBsum; 3LVJ; -.
DR PDBsum; 3LVK; -.
DR AlphaFoldDB; P0A892; -.
DR SMR; P0A892; -.
DR DIP; DIP-58574N; -.
DR IntAct; P0A892; 1.
DR STRING; 155864.EDL933_4683; -.
DR EnsemblBacteria; AAG58579; AAG58579; Z4844.
DR EnsemblBacteria; BAB37742; BAB37742; ECs_4319.
DR GeneID; 67417100; -.
DR GeneID; 915823; -.
DR KEGG; ece:Z4844; -.
DR KEGG; ecs:ECs_4319; -.
DR PATRIC; fig|386585.9.peg.4512; -.
DR eggNOG; COG0425; Bacteria.
DR HOGENOM; CLU_165255_5_0_6; -.
DR OMA; FCQFLGH; -.
DR EvolutionaryTrace; P0A892; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097163; F:sulfur carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
DR CDD; cd03423; SirA; 1.
DR Gene3D; 3.30.110.40; -; 1.
DR HAMAP; MF_00413; Thiourid_synth_A; 1.
DR InterPro; IPR022931; Sulphur_carrier_TusA.
DR InterPro; IPR001455; TusA-like.
DR InterPro; IPR036868; TusA-like_sf.
DR Pfam; PF01206; TusA; 1.
DR SUPFAM; SSF64307; SSF64307; 1.
DR PROSITE; PS01148; UPF0033; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; tRNA processing.
FT CHAIN 1..81
FT /note="Sulfur carrier protein TusA"
FT /id="PRO_0000159034"
FT ACT_SITE 19
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00413"
FT MUTAGEN 21
FT /note="E->A: Decreased binding of IscS."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 24
FT /note="M->R: No binding of IscS, 50% modified tRNA
FT produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 27..35
FT /note="RKTVRNMQP->DKTVRNMQS: No modified tRNA produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 27
FT /note="R->D,E: No binding of IscS, 19% modified tRNA
FT produced (for R27E)."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 31
FT /note="R->A: No binding of IscS, 30% modified tRNA
FT produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 45
FT /note="D->A: Binds IscS, 56% modified tRNA produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 50
FT /note="R->A: Binds IscS, 67% modified tRNA produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 51
FT /note="D->A: Binds IscS, 67% modified tRNA produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 58
FT /note="F->A: No binding of IscS, 67% modified tRNA
FT produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3LVJ"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:3LVJ"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3LVJ"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:3LVJ"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3LVJ"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3LVJ"
SQ SEQUENCE 81 AA; 9095 MW; 63AA7DE4816A3274 CRC64;
MTDLFSSPDH TLDALGLRCP EPVMMVRKTV RNMQPGETLL IIADDPATTR DIPGFCTFME
HELVAKETDG LPYRYLIRKG G
