ID   TUSA_PECAS              Reviewed;          81 AA.
AC   Q6CZ00;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
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}; OrderedLocusNames=ECA4353;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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   -!- PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_00413}.
CC   -!- SUBUNIT: Interacts with IscS. {ECO:0000255|HAMAP-Rule:MF_00413}.
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; BX950851; CAG77250.1; -; Genomic_DNA.
DR   RefSeq; WP_011095816.1; NC_004547.2.
DR   AlphaFoldDB; Q6CZ00; -.
DR   SMR; Q6CZ00; -.
DR   STRING; 218491.ECA4353; -.
DR   EnsemblBacteria; CAG77250; CAG77250; ECA4353.
DR   KEGG; eca:ECA4353; -.
DR   eggNOG; COG0425; Bacteria.
DR   HOGENOM; CLU_165255_5_0_6; -.
DR   OMA; FCQFLGH; -.
DR   OrthoDB; 2042068at2; -.
DR   Proteomes; UP000007966; 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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..81
FT                   /note="Sulfur carrier protein TusA"
FT                   /id="PRO_0000159036"
FT   ACT_SITE        19
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00413"
SQ   SEQUENCE   81 AA;  9314 MW;  C7426D903315D145 CRC64;
     MTDPFTNPDK TLDAQGLRCP EPVMMVRKTV RQMETGQTLL IIADDPATTR DIPGFCVYME
     HELLAQETEQ VPYRYLLRKG Q