RESA_BACSU
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 03-AUG-2022, entry version 155.
DE RecName: Full=Thiol-disulfide oxidoreductase ResA;
GN Name=resA; Synonyms=ypxA; OrderedLocusNames=BSU23150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; 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 / NCIMB
RC 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 RefSeq; WP_009967646.1; NZ_CM000487.1.
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 PRIDE; P35160; -.
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 OMA; MIGKPFP; -.
DR PhylomeDB; P35160; -.
DR BioCyc; BSUB:BSU23150-MON; -.
DR BioCyc; MetaCyc:BSU23150-MON; -.
DR UniPathway; UPA00555; -.
DR EvolutionaryTrace; P35160; -.
DR Proteomes; UP000001570; 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 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
