ID   RESA_ALKCK              Reviewed;         177 AA.
AC   Q5WGY8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Probable thiol-disulfide oxidoreductase ResA;
GN   Name=resA; OrderedLocusNames=ABC1832;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; cytochrome c assembly.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}. Note=The thioredoxin-like motif is
CC       exposed on the outside of the membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. ResA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP006627; BAD64367.1; -; Genomic_DNA.
DR   RefSeq; WP_011246675.1; NC_006582.1.
DR   AlphaFoldDB; Q5WGY8; -.
DR   SMR; Q5WGY8; -.
DR   STRING; 66692.ABC1832; -.
DR   EnsemblBacteria; BAD64367; BAD64367; ABC1832.
DR   KEGG; bcl:ABC1832; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_2_9; -.
DR   OMA; LVYQIMS; -.
DR   OrthoDB; 1617952at2; -.
DR   UniPathway; UPA00555; -.
DR   Proteomes; UP000001168; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF08534; Redoxin; 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..177
FT                   /note="Probable thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000308267"
FT   TRANSMEM        13..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          38..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        76..79
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   177 AA;  19836 MW;  21ED2C167B2E4779 CRC64;
     MGKSKKKRSI IRFTVLFAIV CAIGYTIYAN AASEQGAVKV GEPATNFALV DLEQERFELG
     QNQGKGVFIN FWGTFCEPCE REMPYIENAY EQYKDEVEMI AVNVDEAPLT VQSFINRHGL
     TFPVAIDERR EVTRAYGIGP LPATILVDEH GIVQKVHTGA MTEEMVHEFF QSIVPDA