RESA_BACAH
ID RESA_BACAH Reviewed; 173 AA.
AC A0RBT0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN Name=resA {ECO:0000255|HAMAP-Rule:MF_01319}; OrderedLocusNames=BALH_1330;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK84673.1; -; Genomic_DNA.
DR RefSeq; WP_000742206.1; NC_008600.1.
DR AlphaFoldDB; A0RBT0; -.
DR SMR; A0RBT0; -.
DR EnsemblBacteria; ABK84673; ABK84673; BALH_1330.
DR GeneID; 45021470; -.
DR KEGG; btl:BALH_1330; -.
DR HOGENOM; CLU_042529_11_2_9; -.
DR OMA; MIGKPFP; -.
DR UniPathway; UPA00555; -.
DR Proteomes; UP000000761; 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_0000308269"
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; 19587 MW; 960D8021E4497474 CRC64;
MKKNRLLFRV IILLILSGAV GFTLYQGFFA DKEKMQIGKE APNFVVTDLE GKKIELKDLK
GKGVFLNFWG TWCKPCEKEM PYMNELYPKY KEKGVEIIAL DADETDIAVK NFVNQYGLKF
PVAIDKGQKI IGTYGVGPLP TSFLIDKDGK VVEQIIGEQT KEQLEGYLKK ITP