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Database: UniProt
Entry: A0A0T6A8W7_9BACT
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ID   A0A0T6A8W7_9BACT        Unreviewed;       441 AA.
AC   A0A0T6A8W7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=L-cysteine S-thiosulfotransferase subunit SoxA {ECO:0000256|ARBA:ARBA00019364};
DE            EC=2.8.5.2 {ECO:0000256|ARBA:ARBA00012408};
GN   ORFNames=XU13_C0051G0005 {ECO:0000313|EMBL:KRT71358.1};
OS   Candidatus Rokubacteria bacterium CSP1-6.
OC   Bacteria; Candidatus Rokubacteria.
OX   NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT71358.1, ECO:0000313|Proteomes:UP000051916};
RN   [1] {ECO:0000313|EMBL:KRT71358.1, ECO:0000313|Proteomes:UP000051916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT71358.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] +
CC         thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-
CC         cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00029285};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY
CC         protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-
CC         sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689,
CC         Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963,
CC         ChEBI:CHEBI:140664; EC=2.8.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00029308};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the SoxA family.
CC       {ECO:0000256|ARBA:ARBA00025746}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRT71358.1}.
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DR   EMBL; LDXP01000051; KRT71358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6A8W7; -.
DR   STRING; 1640509.XU13_C0051G0005; -.
DR   Proteomes; UP000051916; Unassembled WGS sequence.
DR   GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016669; F:oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019417; P:sulfur oxidation; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 3.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR025710; SoxA.
DR   InterPro; IPR030999; Thiosulf_SoxX.
DR   NCBIfam; TIGR04484; thiosulf_SoxA; 1.
DR   NCBIfam; TIGR04485; thiosulf_SoxX; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF21342; SoxA-TsdA_cyt-c; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 3.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..441
FT                   /note="L-cysteine S-thiosulfotransferase subunit SoxA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006667677"
FT   DOMAIN          102..194
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          195..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  48213 MW;  4E32F51F02EEC28F CRC64;
     MLRPGTVFGG GIVFAALLSA ACAQTDKAST AGLPPAPWIS RAIPEGKGEV KTQPDGKKMQ
     VRYKRAPFAG VPQDWSDYRT YAYDDTRPAP PVSKAPMTQV KGDPARGRRL FLSRAQGPCT
     GCHLIPGADV WPAGNIGPDL STYGDRNLPD EFIFTQLYDS RNFFPHTTMP PWGTTGVFKP
     EELVHIVAFL KTLKGPVPPE KDPDRNPDTR AKPVGFGDNL DPTNNPAVLL AEGAMAVWSK
     KGPAGKACAD CHAGGPEKSM KEAATRYPKY VKAYQRVMSI EDFLTVHAPE TTGLQMLSQS
     ADNLNMTMLV KMQSNGMPLK VDVTSPEAKG AYERGRASFF KRVGQRNHAC ADCHTKGAGR
     GSDKFLGGRL LADVEVGLTK HFPLWRTSQG QVWDMRKRMQ WCMTPLGMNM LPADAVEYAE
     LELYLTAFDN GKEMSVPGIR H
//
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