ID   RESA_BACLD              Reviewed;         177 AA.
AC   Q65HX8; Q62TC7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   Name=resA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   OrderedLocusNames=BLi02461, BL00661;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU23982.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU41336.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q65HX8; -.
DR   SMR; Q65HX8; -.
DR   STRING; 279010.BL00661; -.
DR   EnsemblBacteria; AAU23982; AAU23982; BL00661.
DR   KEGG; bld:BLi02461; -.
DR   KEGG; bli:BL00661; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_2_9; -.
DR   OMA; MIGKPFP; -.
DR   OrthoDB; 1617952at2; -.
DR   BioCyc; BLIC279010:BLI_RS12190-MON; -.
DR   UniPathway; UPA00555; -.
DR   Proteomes; UP000000606; 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..177
FT                   /note="Thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000308268"
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   177 AA;  20048 MW;  A735E9B1F55C3391 CRC64;
     MKKKRFYIRT GILLVLLAAL GYTLYSAVFQ NTESVAVGEK APIFSLEDVD GNRLKLDELK
     GKGVFLNFWG TWCEPCKREF PYMANQYKVF KDKGVEIVAV NVGESNLAVR NFMKDHGVNF
     PVVLDKDRQV LNAYDVTPLP TTFLINPDGE IVKVVTGEMT ERMIHDYMNM IKPEGSS