ID   TUSA_ALLVD              Reviewed;          76 AA.
AC   D3RPC0;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Sulfur carrier protein TusA {ECO:0000305|PubMed:24648525};
GN   Name=tusA {ECO:0000303|PubMed:24648525};
GN   OrderedLocusNames=Alvin_2600 {ECO:0000312|EMBL:ADC63510.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=24487535; DOI=10.1128/aem.04182-13;
RA   Weissgerber T., Sylvester M., Kroeninger L., Dahl C.;
RT   "A comparative quantitative proteomic study identifies new proteins
RT   relevant for sulfur oxidation in the purple sulfur bacterium Allochromatium
RT   vinosum.";
RL   Appl. Environ. Microbiol. 80:2279-2292(2014).
RN   [3]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, PATHWAY,
RP   SUBUNIT, SULFUR-BINDING, MUTAGENESIS OF CYS-15, INTERACTION WITH DSREFH,
RP   AND ACTIVE SITE.
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=24648525; DOI=10.1074/jbc.m113.536425;
RA   Stockdreher Y., Sturm M., Josten M., Sahl H.G., Dobler N., Zigann R.,
RA   Dahl C.;
RT   "New proteins involved in sulfur trafficking in the cytoplasm of
RT   Allochromatium vinosum.";
RL   J. Biol. Chem. 289:12390-12403(2014).
CC   -!- FUNCTION: Sulfur carrier protein involved in sulfur trafficking for
CC       oxidative dissimilatory sulfur metabolism. Component of a sulfur relay
CC       system that starts with the sulfur-mobilizing rhodanese-like protein
CC       Rhd_2599 (Alvin_2599), which transfers the sulfur from a low-molecular-
CC       weight thiol, maybe glutathione, to the TusA protein (Alvin_2600); TusA
CC       serves as the sulfur donor for DsrEFH, which persulfurates DsrC;
CC       persulfurated DsrC very probably serves as a direct substrate for
CC       reverse-acting sulfite reductase, DsrAB. TusA seems to be not
CC       exclusively dedicated to sulfur oxidation and may have other important
CC       roles in the cell. Might also act as a sulfur mediator required for 2-
CC       thiouridine formation of tRNA. {ECO:0000269|PubMed:24648525,
CC       ECO:0000305}.
CC   -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC       {ECO:0000305|PubMed:24648525}.
CC   -!- SUBUNIT: Mostly a monomer, a small portion forms homodimer via
CC       intermolecular disulfide bonds. Tightly interacts with DsrEFH.
CC       {ECO:0000269|PubMed:24648525}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24648525}.
CC   -!- INDUCTION: Up-regulated under sulfur-oxidizing conditions (at mRNA
CC       level), i.e. when grown on reduced sulfur compounds such as sulfide,
CC       thiosulfate or elemental sulfur (PubMed:24648525). TusA is one of the
CC       major proteins in A.vinosum cells grown on malate or on reduced sulfur
CC       compounds (PubMed:24487535). {ECO:0000269|PubMed:24487535,
CC       ECO:0000269|PubMed:24648525}.
CC   -!- DISRUPTION PHENOTYPE: A mutant strain lacking rhd_2599, tusA and dsrE2,
CC       although not viable in liquid culture, is clearly sulfur oxidation
CC       negative upon growth on solid media containing sulfide, and shows
CC       massive accumulation of intercellular sulfur globules.
CC       {ECO:0000269|PubMed:24648525}.
CC   -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC       {ECO:0000305}.
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DR   EMBL; CP001896; ADC63510.1; -; Genomic_DNA.
DR   RefSeq; WP_012971778.1; NC_013851.1.
DR   AlphaFoldDB; D3RPC0; -.
DR   SMR; D3RPC0; -.
DR   STRING; 572477.Alvin_2600; -.
DR   EnsemblBacteria; ADC63510; ADC63510; Alvin_2600.
DR   KEGG; alv:Alvin_2600; -.
DR   eggNOG; COG0425; Bacteria.
DR   HOGENOM; CLU_165255_1_2_6; -.
DR   OMA; NDMASWA; -.
DR   OrthoDB; 2042068at2; -.
DR   BioCyc; MetaCyc:MON-19178; -.
DR   UniPathway; UPA00096; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.110.40; -; 1.
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   Cytoplasm; Disulfide bond; Reference proteome.
FT   CHAIN           1..76
FT                   /note="Sulfur carrier protein TusA"
FT                   /id="PRO_0000439098"
FT   ACT_SITE        15
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000269|PubMed:24648525"
FT   MUTAGEN         15
FT                   /note="C->S: Loss of sulfur binding in the presence of
FT                   sulfide. Loss of interaction with DsrEFH proteins."
FT                   /evidence="ECO:0000269|PubMed:24648525"
SQ   SEQUENCE   76 AA;  8268 MW;  0495B6B6548D0104 CRC64;
     MADFDQELDA SGLNCPLPIL RAKKTLNAMS SGQVLHVIAT DPGSVKDFDA FAKQTGNELM
     ESKEEGGKFH FLIKKS