ID   RESA_BACCZ              Reviewed;         173 AA.
AC   Q63DQ8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   Name=resA {ECO:0000255|HAMAP-Rule:MF_01319}; OrderedLocusNames=BCE33L1355;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU18893.1; -; Genomic_DNA.
DR   RefSeq; WP_000742191.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q63DQ8; -.
DR   SMR; Q63DQ8; -.
DR   EnsemblBacteria; AAU18893; AAU18893; BCE33L1355.
DR   GeneID; 56651328; -.
DR   KEGG; bcz:BCE33L1355; -.
DR   PATRIC; fig|288681.22.peg.4197; -.
DR   OMA; MIGKPFP; -.
DR   UniPathway; UPA00555; -.
DR   Proteomes; UP000002612; 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; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..173
FT                   /note="Thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000120147"
FT   TRANSMEM        10..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT   DOMAIN          35..173
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT   DISULFID        73..76
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
SQ   SEQUENCE   173 AA;  19692 MW;  A3BA9A873CCDD28D CRC64;
     MKKNRLLFRV IILLILCGAV GFTLYQGFFA DKEKMQIGKE APNFVVTDLE GKKIELKDLK
     GKGVFLNFWG TWCKPCEKEM PYMNELYPKY KEKGVEIIAL DADETEIAVK NFVKQYDLKF
     PVAIDKGTKI IGTYSVGPLP TSFLIDKDGK VVEKIIGEQT KEQLEGYLQK ITP