ID   RESA_BACSU              Reviewed;         179 AA.
AC   P35160;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Thiol-disulfide oxidoreductase ResA;
GN   Name=resA; Synonyms=ypxA; OrderedLocusNames=BSU23150;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA   Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT   "The organization of the Bacillus subtilis 168 chromosome region between
RT   the spoVA and serA genetic loci, based on sequence data.";
RL   Mol. Microbiol. 10:385-395(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   GENE NAME.
RX   PubMed=8631715; DOI=10.1128/jb.178.5.1374-1385.1996;
RA   Sun G., Sharkova E., Chesnut R., Birkey S., Duggan M.F., Sorokin A.V.,
RA   Pujic P., Ehrlich S.D., Hulett F.M.;
RT   "Regulators of aerobic and anaerobic respiration in Bacillus subtilis.";
RL   J. Bacteriol. 178:1374-1385(1996).
RN   [5]
RP   DETECTION OF FRAMESHIFT, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=12637552; DOI=10.1074/jbc.m300103200;
RA   Erlendsson L.S., Acheson R.M., Hederstedt L., Le Brun N.E.;
RT   "Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in
RT   cytochrome c synthesis.";
RL   J. Biol. Chem. 278:17852-17858(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 37-179 IN THE OXIDIZED AND REDUCED
RP   STATES.
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=15047692; DOI=10.1074/jbc.m402823200;
RA   Crow A., Acheson R.M., Le Brun N.E., Oubrie A.;
RT   "Structural basis of redox-coupled protein substrate selection by the
RT   cytochrome c biosynthesis protein ResA.";
RL   J. Biol. Chem. 279:23654-23660(2004).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-179 WITH CYSTEINE MUTATIONS,
RP   AND CRYSTALLIZED AT HIGH PH.
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=16971393; DOI=10.1074/jbc.m607047200;
RA   Lewin A., Crow A., Oubrie A., Le Brun N.E.;
RT   "Molecular basis for specificity of the extracytoplasmic thioredoxin
RT   ResA.";
RL   J. Biol. Chem. 281:35467-35477(2006).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 37-179, AND NMR.
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=16537372; DOI=10.1073/pnas.0600552103;
RA   Colbert C.L., Wu Q., Erbel P.J.A., Gardner K.H., Deisenhofer J.;
RT   "Mechanism of substrate specificity in Bacillus subtilis ResA, a
RT   thioredoxin-like protein involved in cytochrome c maturation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:4410-4415(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. Does not play a role in sporulation.
CC       {ECO:0000269|PubMed:12637552}.
CC   -!- PATHWAY: Protein modification; cytochrome c assembly.
CC   -!- INTERACTION:
CC       P35160; P24469: cccA; NbExp=2; IntAct=EBI-15573707, EBI-15573689;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12637552};
CC       Single-pass type II membrane protein {ECO:0000269|PubMed:12637552}.
CC       Note=The thioredoxin-like motif is exposed on the outside of the
CC       membrane.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. ResA subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA67494.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L09228; AAA67494.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB14247.2; -; Genomic_DNA.
DR   PIR; S45556; S45556.
DR   RefSeq; NP_390196.2; NC_000964.3.
DR   RefSeq; WP_003230513.1; NZ_JNCM01000036.1.
DR   PDB; 1ST9; X-ray; 1.50 A; A/B=37-179.
DR   PDB; 1SU9; X-ray; 1.95 A; A/B=37-179.
DR   PDB; 2F9S; X-ray; 1.40 A; A/B=37-179.
DR   PDB; 2H19; X-ray; 2.00 A; A/B=37-179.
DR   PDB; 2H1A; X-ray; 2.40 A; A/B=37-179.
DR   PDB; 2H1B; X-ray; 1.95 A; A/B/C/D=37-179.
DR   PDB; 2H1D; X-ray; 2.60 A; A/B=37-179.
DR   PDB; 2H1G; X-ray; 3.10 A; A/B=37-179.
DR   PDB; 3C71; X-ray; 1.90 A; A=37-179.
DR   PDB; 3C73; X-ray; 2.50 A; A/B=40-179.
DR   PDBsum; 1ST9; -.
DR   PDBsum; 1SU9; -.
DR   PDBsum; 2F9S; -.
DR   PDBsum; 2H19; -.
DR   PDBsum; 2H1A; -.
DR   PDBsum; 2H1B; -.
DR   PDBsum; 2H1D; -.
DR   PDBsum; 2H1G; -.
DR   PDBsum; 3C71; -.
DR   PDBsum; 3C73; -.
DR   AlphaFoldDB; P35160; -.
DR   SMR; P35160; -.
DR   DIP; DIP-61132N; -.
DR   IntAct; P35160; 1.
DR   STRING; 224308.BSU23150; -.
DR   PaxDb; 224308-BSU23150; -.
DR   EnsemblBacteria; CAB14247; CAB14247; BSU_23150.
DR   GeneID; 938958; -.
DR   KEGG; bsu:BSU23150; -.
DR   PATRIC; fig|224308.179.peg.2522; -.
DR   eggNOG; COG0526; Bacteria.
DR   InParanoid; P35160; -.
DR   OrthoDB; 25753at2; -.
DR   PhylomeDB; P35160; -.
DR   BioCyc; BSUB:BSU23150-MONOMER; -.
DR   BioCyc; MetaCyc:BSU23150-MONOMER; -.
DR   UniPathway; UPA00555; -.
DR   EvolutionaryTrace; P35160; -.
DR   Proteomes; UP000001570; Chromosome.
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   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 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..179
FT                   /note="Thiol-disulfide oxidoreductase ResA"
FT                   /id="PRO_0000120149"
FT   TRANSMEM        11..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          36..174
FT                   /note="Thioredoxin"
FT   DISULFID        74..77
FT                   /note="Redox-active"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   HELIX           75..91
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   HELIX           107..117
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   STRAND          142..146
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   STRAND          150..158
FT                   /evidence="ECO:0007829|PDB:2F9S"
FT   HELIX           162..172
FT                   /evidence="ECO:0007829|PDB:2F9S"
SQ   SEQUENCE   179 AA;  20008 MW;  E023A46F4BD702AC CRC64;
     MKKKRRLFIR TGILLVLICA LGYTIYNAVF AGKESISEGS DAPNFVLEDT NGKRIELSDL
     KGKGVFLNFW GTWCEPCKKE FPYMANQYKH FKSQGVEIVA VNVGESKIAV HNFMKSYGVN
     FPVVLDTDRQ VLDAYDVSPL PTTFLINPEG KVVKVVTGTM TESMIHDYMN LIKPGETSG
//