ID   CYCY_RHILV              Reviewed;         186 AA.
AC   P45409;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 98.
DE   RecName: Full=Thiol:disulfide interchange protein CycY;
DE   AltName: Full=Cytochrome c biogenesis protein CycY;
DE   Flags: Precursor;
GN   Name=cycY;
OS   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=8021193; DOI=10.1128/jb.176.13.4117-4123.1994;
RA   Vargas C., Wu G., Davies A.E., Downie J.A.;
RT   "Identification of a gene encoding a thioredoxin-like product necessary for
RT   cytochrome c biosynthesis and symbiotic nitrogen fixation in Rhizobium
RT   leguminosarum.";
RL   J. Bacteriol. 176:4117-4123(1994).
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X79307; CAB61632.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45409; -.
DR   SMR; P45409; -.
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:InterPro.
DR   CDD; cd03010; TlpA_like_DsbE; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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   InterPro; IPR050553; Thioredoxin_ResA/DsbE_sf.
DR   NCBIfam; TIGR00385; dsbE; 1.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..186
FT                   /note="Thiol:disulfide interchange protein CycY"
FT                   /id="PRO_0000034288"
FT   DOMAIN          47..182
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        80..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   186 AA;  19836 MW;  7A0EC95D5B906E26 CRC64;
     MGRYTLALLP LIVFGGIAHG AKMLYDQDFH GKNIAEIPSA LSHQGADAEP AAARRATLPA
     LTDAAIKGKL TLVNVFASWC LPCRDEHPVL KELAKDGRLN IVAINYKDQS DNALRFLGEL
     GNPYQAIGID PNGKAAIDWG VYGIPESYLV GADGTILYKR VGPSTNISLK EGLVPAMEKA
     LGKPVS
//