RESA_BACCR
ID RESA_BACCR Reviewed; 173 AA.
AC Q81FU5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN Name=resA {ECO:0000255|HAMAP-Rule:MF_01319}; OrderedLocusNames=BC_1473;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP08453.1; -; Genomic_DNA.
DR RefSeq; NP_831252.1; NC_004722.1.
DR RefSeq; WP_000742192.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81FU5; -.
DR SMR; Q81FU5; -.
DR STRING; 226900.BC_1473; -.
DR EnsemblBacteria; AAP08453; AAP08453; BC_1473.
DR GeneID; 67506175; -.
DR KEGG; bce:BC1473; -.
DR PATRIC; fig|226900.8.peg.1450; -.
DR HOGENOM; CLU_042529_11_2_9; -.
DR OMA; MIGKPFP; -.
DR UniPathway; UPA00555; -.
DR Proteomes; UP000001417; 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; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..173
FT /note="Thiol-disulfide oxidoreductase ResA"
FT /id="PRO_0000120146"
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; 19616 MW; D053E8004994A92A CRC64;
MKKNRLLFRV IILLILCGAV GFTLYQGFFA NKEKMQIGKE APNFIVTDLE GKKIELKDLK
GKGVFLNFWG TWCKPCEKEM PYMNELYPKY KEKGVEIIAL DADETDIAVK NFVNQYGLKF
PVAIDKGQKI IGTYGVGPLP TSFLIDKDGK VVEQIIGEQT KEQLEGYLKK ITP