RESA_BACC1
ID RESA_BACC1 Reviewed; 173 AA.
AC Q73B22;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-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=BCE_1598;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(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; AE017194; AAS40527.1; -; Genomic_DNA.
DR RefSeq; WP_000742210.1; NC_003909.8.
DR AlphaFoldDB; Q73B22; -.
DR SMR; Q73B22; -.
DR EnsemblBacteria; AAS40527; AAS40527; BCE_1598.
DR GeneID; 59158244; -.
DR KEGG; bca:BCE_1598; -.
DR HOGENOM; CLU_042529_11_2_9; -.
DR OMA; MIGKPFP; -.
DR UniPathway; UPA00555; -.
DR Proteomes; UP000002527; 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_0000308266"
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; 19898 MW; 94B92C452EF11F47 CRC64;
MKKNRLLFRV IILLILSGAV GFTLYQGYFS KEEKMEIGKE APNFVVTDLE GKKIELKDFK
GKGVFLNFWG TWCKPCEKEM PYMNELYPKY KEKGVEIIAL DADETDIAVK NFVKQYDLKF
PVAIDKGGEI IKTYGVIPLP TSFLIDKDGK VIQEIKGEQT KEQLEEYLKK ITP
