ID   RESA_ALKHC              Reviewed;         176 AA.
AC   Q9KCJ4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   Name=resA {ECO:0000255|HAMAP-Rule:MF_01319}; OrderedLocusNames=BH1577;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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}.
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DR   EMBL; BA000004; BAB05296.1; -; Genomic_DNA.
DR   PIR; A83847; A83847.
DR   RefSeq; WP_010897740.1; NC_002570.2.
DR   AlphaFoldDB; Q9KCJ4; -.
DR   SMR; Q9KCJ4; -.
DR   STRING; 272558.10174194; -.
DR   EnsemblBacteria; BAB05296; BAB05296; BAB05296.
DR   KEGG; bha:BH1577; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_2_9; -.
DR   OMA; LVYQIMS; -.
DR   OrthoDB; 1617952at2; -.
DR   UniPathway; UPA00555; -.
DR   Proteomes; UP000001258; 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; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 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..176
FT                   /note="Thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000120148"
FT   TRANSMEM        11..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT   DOMAIN          36..176
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT   DISULFID        74..77
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
SQ   SEQUENCE   176 AA;  20156 MW;  6A144E2A7D205CCE CRC64;
     MDKRKRFWMR LSILAVISVA LGYTFYSNFF ADRSLARAGE QAVNFVLEDL EGESIELREL
     EGKGVFLNFW GTYCPPCERE MPHMEKLYGE YKEQGVEIIA VNANEPELTV QRFVDRYGLS
     FPIVIDKGLN VIDAYGIRPL PTTILINEHG EIVKVHTGGM TEQMVEEFME LIKPEA