ID   RESA_BACAN              Reviewed;         173 AA.
AC   Q81SZ9; Q6I179; Q6KV30;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   Name=resA {ECO:0000255|HAMAP-Rule:MF_01319};
GN   OrderedLocusNames=BA_1494, GBAA_1494, BAS1383;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) 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. {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; AE016879; AAP25432.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT30592.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT53703.1; -; Genomic_DNA.
DR   RefSeq; NP_843946.1; NC_003997.3.
DR   RefSeq; WP_000742206.1; NZ_WXXJ01000014.1.
DR   RefSeq; YP_027652.1; NC_005945.1.
DR   PDB; 4NMU; X-ray; 1.35 A; A/B/C/D=30-173.
DR   PDBsum; 4NMU; -.
DR   AlphaFoldDB; Q81SZ9; -.
DR   SMR; Q81SZ9; -.
DR   STRING; 261594.GBAA_1494; -.
DR   DNASU; 1086435; -.
DR   EnsemblBacteria; AAP25432; AAP25432; BA_1494.
DR   EnsemblBacteria; AAT30592; AAT30592; GBAA_1494.
DR   GeneID; 45021470; -.
DR   KEGG; ban:BA_1494; -.
DR   KEGG; bar:GBAA_1494; -.
DR   KEGG; bat:BAS1383; -.
DR   PATRIC; fig|198094.11.peg.1466; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_2_9; -.
DR   OMA; MIGKPFP; -.
DR   UniPathway; UPA00555; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytochrome c-type biogenesis; Disulfide bond;
KW   Membrane; Oxidoreductase; Redox-active center; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..173
FT                   /note="Thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000120145"
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"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          62..69
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   HELIX           74..92
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   HELIX           106..116
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   HELIX           129..134
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   STRAND          149..157
FT                   /evidence="ECO:0007829|PDB:4NMU"
FT   HELIX           161..170
FT                   /evidence="ECO:0007829|PDB:4NMU"
SQ   SEQUENCE   173 AA;  19587 MW;  960D8021E4497474 CRC64;
     MKKNRLLFRV IILLILSGAV GFTLYQGFFA DKEKMQIGKE APNFVVTDLE GKKIELKDLK
     GKGVFLNFWG TWCKPCEKEM PYMNELYPKY KEKGVEIIAL DADETDIAVK NFVNQYGLKF
     PVAIDKGQKI IGTYGVGPLP TSFLIDKDGK VVEQIIGEQT KEQLEGYLKK ITP