RESA_GEOTN
ID RESA_GEOTN Reviewed; 174 AA.
AC A4IQF5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000255|HAMAP-Rule:MF_01319};
GN Name=resA {ECO:0000255|HAMAP-Rule:MF_01319}; OrderedLocusNames=GTNG_2210;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000557; ABO67559.1; -; Genomic_DNA.
DR RefSeq; WP_011887723.1; NC_009328.1.
DR AlphaFoldDB; A4IQF5; -.
DR SMR; A4IQF5; -.
DR STRING; 420246.GTNG_2210; -.
DR EnsemblBacteria; ABO67559; ABO67559; GTNG_2210.
DR KEGG; gtn:GTNG_2210; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_11_2_9; -.
DR OMA; MIGKPFP; -.
DR OrthoDB; 1617952at2; -.
DR UniPathway; UPA00555; -.
DR Proteomes; UP000001578; 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..174
FT /note="Thiol-disulfide oxidoreductase ResA"
FT /id="PRO_0000308272"
FT TRANSMEM 11..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT DOMAIN 36..174
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
FT DISULFID 74..77
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01319"
SQ SEQUENCE 174 AA; 19830 MW; 13C0950F25949111 CRC64;
MKKQQRLVMR TVILLLLLAA LGYTIYANFF TEKTAVAVGS TAPDFVLSDL EGREHRLTDY
RGKGVFLNFW GTWCKPCERE MPYMNELYPI YQKQGVEILA VNVGEPKLNV EKFAERFGLT
FPIVIDRQDQ VLNAYGVGPL PTTFLIDKNG KVKKIITGTM TKEDIKQHLE SIKP
