ID   TSDB_THIK1              Reviewed;         217 AA.
AC   D5WYQ6;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Thiosulfate dehydrogenase electron acceptor;
DE   Flags: Precursor;
GN   Name=tsdB; OrderedLocusNames=Tint_2893;
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=75379;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=22779704; DOI=10.1111/j.1462-2920.2012.02820.x;
RA   Denkmann K., Grein F., Zigann R., Siemen A., Bergmann J., van Helmont S.,
RA   Nicolai A., Pereira I.A., Dahl C.;
RT   "Thiosulfate dehydrogenase: a widespread unusual acidophilic c-type
RT   cytochrome.";
RL   Environ. Microbiol. 14:2673-2688(2012).
CC   -!- FUNCTION: Acts as an electron acceptor for the thiosulfate
CC       dehydrogenase TsdA. {ECO:0000269|PubMed:22779704}.
CC   -!- PTM: Binds 2 heme c groups covalently per subunit. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002021; ADG32233.1; -; Genomic_DNA.
DR   RefSeq; WP_013124333.1; NC_014153.1.
DR   AlphaFoldDB; D5WYQ6; -.
DR   SMR; D5WYQ6; -.
DR   STRING; 75379.Tint_2893; -.
DR   EnsemblBacteria; ADG32233; ADG32233; Tint_2893.
DR   KEGG; tin:Tint_2893; -.
DR   eggNOG; COG2863; Bacteria.
DR   HOGENOM; CLU_076280_0_1_4; -.
DR   OMA; QHADYLF; -.
DR   BioCyc; TINT75379:TINT_RS14500-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR024167; Cytochrome_c4-like.
DR   Pfam; PF00034; Cytochrom_C; 2.
DR   PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR   SUPFAM; SSF46626; SSF46626; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Repeat; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..217
FT                   /note="Thiosulfate dehydrogenase electron acceptor"
FT                   /id="PRO_5000590632"
FT   DOMAIN          29..104
FT                   /note="Cytochrome c 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   DOMAIN          116..206
FT                   /note="Cytochrome c 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         37
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         40
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         41
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         137
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         140
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         141
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   217 AA;  22466 MW;  5B94596C973DE160 CRC64;
     MRQFIPMRRV LAVATLGALF WAAPASWAAA PPEAASCIAC HGAGGMGNPA AGYPRLAGLP
     EQYLADQLRY FADGARNNAV MSGMAKPLSA AQVTALATYY SKLKPSGKPA PMPTGAAAAE
     GERLALRGDW EKGIPACIRC HGPGAVGVGE NFPALVGQSA AYIEAQIKAW KDGSRSGDPL
     GLMHTVALRM TDAQTQAVAQ WLAAQPLSPT KSASAKH