TUSA_ECOLI
ID TUSA_ECOLI Reviewed; 81 AA.
AC P0A890; P37618; Q2M7D3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sulfur carrier protein TusA {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000303|PubMed:23281480};
DE AltName: Full=Sulfur mediator TusA {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000303|PubMed:16387657};
DE AltName: Full=Sulfur transfer protein TusA {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000303|PubMed:23281480};
DE AltName: Full=tRNA 2-thiouridine synthesizing protein A {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000303|PubMed:16387657};
GN Name=tusA {ECO:0000255|HAMAP-Rule:MF_00413, ECO:0000303|PubMed:16387657};
GN Synonyms=sirA, yhhP; OrderedLocusNames=b3470, JW3435;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-21.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9555915; DOI=10.1128/jb.180.8.2257-2261.1998;
RA Yamashino T., Isomura M., Ueguchi C., Mizuno T.;
RT "The yhhP gene encoding a small ubiquitous protein is fundamental for
RT normal cell growth of Escherichia coli.";
RL J. Bacteriol. 180:2257-2261(1998).
RN [5]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10830496; DOI=10.1271/bbb.64.799;
RA Ishii Y., Yamada H., Yamashino T., Ohashi K., Katoh E., Shindo H.,
RA Yamazaki T., Mizuno T.;
RT "Deletion of the yhhP gene results in filamentous cell morphology in
RT Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 64:799-807(2000).
RN [6]
RP FUNCTION, INTERACTION WITH ISCS, IDENTIFICATION BY MASS SPECTROMETRY,
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-19 AND CYS-56, PATHWAY, AND ACTIVE
RP SITE.
RX PubMed=16387657; DOI=10.1016/j.molcel.2005.11.001;
RA Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.;
RT "Mechanistic insights into sulfur relay by multiple sulfur mediators
RT involved in thiouridine biosynthesis at tRNA wobble positions.";
RL Mol. Cell 21:97-108(2006).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=11080457; DOI=10.1006/jmbi.2000.4170;
RA Katoh E., Hatta T., Shindo H., Ishii Y., Yamada H., Mizuno T., Yamazaki T.;
RT "High precision NMR structure of YhhP, a novel Escherichia coli protein
RT implicated in cell division.";
RL J. Mol. Biol. 304:219-229(2000).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ISCS.
RC STRAIN=K12 / BW25113;
RX PubMed=23281480; DOI=10.1074/jbc.m112.431569;
RA Dahl J.U., Radon C., Buehning M., Nimtz M., Leichert L.I., Denis Y.,
RA Jourlin-Castelli C., Iobbi-Nivol C., Mejean V., Leimkuehler S.;
RT "The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli
RT that also affects molybdenum cofactor biosynthesis.";
RL J. Biol. Chem. 288:5426-5442(2013).
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
CC (PubMed:16387657). Interacts with IscS and stimulates its cysteine
CC desulfurase activity (PubMed:16387657, PubMed:23281480). 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 (PubMed:16387657). Also appears to be involved in sulfur
CC transfer for the biosynthesis of molybdopterin (PubMed:23281480). Seems
CC to affect the stability of sigma-S, particularly during the logarithmic
CC growth phase (PubMed:9555915). {ECO:0000269|PubMed:16387657,
CC ECO:0000269|PubMed:23281480, ECO:0000269|PubMed:9555915}.
CC -!- PATHWAY: tRNA modification. {ECO:0000255|HAMAP-Rule:MF_00413,
CC ECO:0000269|PubMed:16387657}.
CC -!- SUBUNIT: Interacts with IscS. {ECO:0000255|HAMAP-Rule:MF_00413,
CC ECO:0000269|PubMed:16387657, ECO:0000269|PubMed:23281480}.
CC -!- INTERACTION:
CC P0A890; P0A6B7: iscS; NbExp=7; IntAct=EBI-561780, EBI-550055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00413,
CC ECO:0000269|PubMed:10830496}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not capable of
CC growing in standard laboratory rich medium (i.e., Luria broth), and
CC show filamentous shape (PubMed:9555915). FtsZ-ring formation appears to
CC be severely impaired in tusA-deficient cells, resulting in the
CC formation of a non-divided filamentous cell (PubMed:10830496). A tusA
CC deletion mutant lacks the 2-thio modification of mnm5s2U in tRNA and
CC has a severe growth defect (PubMed:16387657). Deletion of tusA has a
CC pleiotropic effect on transcription, including increased expression of
CC molybdenum cofactor biosynthesis genes (moaABCDE operon), but leads to
CC reduced activity of molybdoenzymes, an overall low molybdopterin
CC content and an accumulation of the molybdopterin precursor cyclic
CC pyranopterin monophopshate (cPMP) (PubMed:23281480).
CC {ECO:0000269|PubMed:10830496, ECO:0000269|PubMed:16387657,
CC ECO:0000269|PubMed:23281480, ECO:0000269|PubMed:9555915}.
CC -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC {ECO:0000255|HAMAP-Rule:MF_00413}.
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DR EMBL; U00039; AAB18445.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76495.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77823.1; -; Genomic_DNA.
DR PIR; S47689; S47689.
DR RefSeq; NP_417927.1; NC_000913.3.
DR RefSeq; WP_000130621.1; NZ_STEB01000004.1.
DR PDB; 1DCJ; NMR; -; A=1-81.
DR PDBsum; 1DCJ; -.
DR AlphaFoldDB; P0A890; -.
DR SMR; P0A890; -.
DR BioGRID; 852283; 1.
DR ComplexPortal; CPX-2139; iscS-tusA cysteine desulfurase complex.
DR DIP; DIP-48202N; -.
DR IntAct; P0A890; 16.
DR STRING; 511145.b3470; -.
DR jPOST; P0A890; -.
DR PaxDb; P0A890; -.
DR PRIDE; P0A890; -.
DR EnsemblBacteria; AAC76495; AAC76495; b3470.
DR EnsemblBacteria; BAE77823; BAE77823; BAE77823.
DR GeneID; 67417100; -.
DR GeneID; 947974; -.
DR KEGG; ecj:JW3435; -.
DR KEGG; eco:b3470; -.
DR PATRIC; fig|1411691.4.peg.3255; -.
DR EchoBASE; EB2130; -.
DR eggNOG; COG0425; Bacteria.
DR HOGENOM; CLU_165255_5_0_6; -.
DR InParanoid; P0A890; -.
DR OMA; FCQFLGH; -.
DR PhylomeDB; P0A890; -.
DR BioCyc; EcoCyc:EG12216-MON; -.
DR BioCyc; MetaCyc:EG12216-MON; -.
DR EvolutionaryTrace; P0A890; -.
DR PRO; PR:P0A890; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990329; C:IscS-TusA complex; IPI:ComplexPortal.
DR GO; GO:0097163; F:sulfur carrier activity; IDA:EcoCyc.
DR GO; GO:0019448; P:L-cysteine catabolic process; IDA:ComplexPortal.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:EcoCyc.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IDA:ComplexPortal.
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_0000159033"
FT ACT_SITE 19
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00413,
FT ECO:0000269|PubMed:16387657"
FT MUTAGEN 19
FT /note="C->S: Unable to restore mnm5s2U formation in a tusA-
FT deficient mutant. Unable to accept sulfur from IscS."
FT /evidence="ECO:0000269|PubMed:16387657"
FT MUTAGEN 21
FT /note="E->K: In sirA1; affects the stability of sigma-S
FT during the logarithmic growth phase."
FT /evidence="ECO:0000269|PubMed:9555915"
FT MUTAGEN 56
FT /note="C->S: Able to restore mnm5s2U formation in a tusA-
FT deficient mutant."
FT /evidence="ECO:0000269|PubMed:16387657"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1DCJ"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1DCJ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1DCJ"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1DCJ"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1DCJ"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:1DCJ"
SQ SEQUENCE 81 AA; 9095 MW; 63AA7DE4816A3274 CRC64;
MTDLFSSPDH TLDALGLRCP EPVMMVRKTV RNMQPGETLL IIADDPATTR DIPGFCTFME
HELVAKETDG LPYRYLIRKG G
