HELX_RHOCB
ID HELX_RHOCB Reviewed; 176 AA.
AC P36893; D5AU95;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Thiol:disulfide interchange protein HelX;
DE AltName: Full=Cytochrome c biogenesis protein HelX;
DE Flags: Precursor;
GN Name=helX; Synonyms=ccmG; OrderedLocusNames=RCAP_rcc01789;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8384715; DOI=10.1073/pnas.90.6.2179;
RA Beckman D.L., Kranz R.G.;
RT "Cytochromes c biogenesis in a photosynthetic bacterium requires a
RT periplasmic thioredoxin-like protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2179-2183(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Also acts as a disulfide oxidoreductase in cytochromes c
CC biogenesis. The cysteines of apocytochromes c must be in the reduced
CC state for covalent linkage between the two moieties to occur (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000305}.
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; M96013; AAA03178.1; -; Unassigned_DNA.
DR EMBL; CP001312; ADE85534.1; -; Genomic_DNA.
DR PIR; A47384; A47384.
DR AlphaFoldDB; P36893; -.
DR SMR; P36893; -.
DR IntAct; P36893; 1.
DR STRING; 272942.RCAP_rcc01789; -.
DR EnsemblBacteria; ADE85534; ADE85534; RCAP_rcc01789.
DR KEGG; rcp:RCAP_rcc01789; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_0_5; -.
DR OMA; MIGKPFP; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR CDD; cd03010; TlpA_like_DsbE; 1.
DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00385; dsbE; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytochrome c-type biogenesis; Disulfide bond; Periplasm;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..176
FT /note="Thiol:disulfide interchange protein HelX"
FT /id="PRO_0000034286"
FT DOMAIN 35..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 75..78
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 176 AA; 18736 MW; 8EBB6BD9E0C2F817 CRC64;
MAKPLMFLPL LVMAGFVGAG YFAMQQNDPN AMPTALAGKE APAVRLEPLG AEAPFTDADL
RDGKIKLVNF WASWCAPCRV EHPNLIGLKQ DGIEIMGVNW KDTPDQAQGF LAEMGSPYTR
LGADPGNKMG LDWGVAGVPE TFVVDGAGRI LTRIAGPLTE DVITKKIDPL LAGTAD
