ID   RESA_OCEIH              Reviewed;         192 AA.
AC   Q8CXF3;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   Name=resA {ECO:0000255|HAMAP-Rule:MF_01319}; OrderedLocusNames=OB1822;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
CC   -!- FUNCTION: Thiol-disulfide oxidoreductase which is required in disulfide
CC       reduction during c-type cytochrome synthesis. May accept reducing
CC       equivalents from CcdA, leading to breakage of disulfide bonds in
CC       apocytochrome c; following this reduction heme can be covalently
CC       attached. {ECO:0000255|HAMAP-Rule:MF_01319}.
CC   -!- PATHWAY: Protein modification; cytochrome c assembly.
CC       {ECO:0000255|HAMAP-Rule:MF_01319}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01319};
CC       Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_01319}.
CC       Note=The thioredoxin-like motif is exposed on the outside of the
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_01319}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. ResA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01319}.
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; BA000028; BAC13778.1; -; Genomic_DNA.
DR   RefSeq; WP_011066220.1; NC_004193.1.
DR   AlphaFoldDB; Q8CXF3; -.
DR   SMR; Q8CXF3; -.
DR   STRING; 221109.22777506; -.
DR   EnsemblBacteria; BAC13778; BAC13778; BAC13778.
DR   KEGG; oih:OB1822; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_2_9; -.
DR   OMA; PAVIVFW; -.
DR   OrthoDB; 1617952at2; -.
DR   PhylomeDB; Q8CXF3; -.
DR   UniPathway; UPA00555; -.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01319; ResA; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR023555; Thiol-dS_OxRdtase_ResA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytochrome c-type biogenesis; Disulfide bond; Membrane;
KW   Oxidoreductase; Redox-active center; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..192
FT                   /note="Thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000120150"
FT   TRANSMEM        22..41
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT   DOMAIN          47..189
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT   DISULFID        89..92
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
SQ   SEQUENCE   192 AA;  21904 MW;  31910F4DC830052F CRC64;
     MDIQQNKTNK QKKKRNRFIF RSSILLILVA AVVFAIVSNM KDDNKIYRVG DAAPDFQLKQ
     ISEEVDQSTV QLSDLEGKGV MLNFWATWCD PCKAEMPYMQ DLYAEYKEKG VEIVAVSLDG
     TELVVDQFID EYDLTFPVPH DKNGEVKDLY KIGPMPTTYF IKPNGEIEEI VQGALTLDRL
     EGYLNDIAPQ QN