CYCY_BRADU
ID CYCY_BRADU Reviewed; 194 AA.
AC P30960;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Thiol:disulfide interchange protein CycY;
DE AltName: Full=Cytochrome c biogenesis protein CycY;
DE Flags: Precursor;
GN Name=cycY; Synonyms=ccmG; OrderedLocusNames=blr0471;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110RIF15;
RX PubMed=1850420; DOI=10.1016/s0021-9258(20)89520-9;
RA Ramseier T.M., Winteler H.V., Hennecke H.;
RT "Discovery and sequence analysis of bacterial genes involved in the
RT biogenesis of c-type cytochromes.";
RL J. Biol. Chem. 266:7793-7803(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 39-194, AND DISULFIDE BOND.
RX PubMed=12121652; DOI=10.1016/s0969-2126(02)00794-3;
RA Edeling M.A., Guddat L.W., Fabianek R.A., Thoeny-Meyer L., Martin J.L.;
RT "Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing
RT activity in an indiscriminately oxidizing environment.";
RL Structure 10:973-979(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60874; AAA26196.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000040; BAC45736.1; -; Genomic_DNA.
DR PIR; D39741; D39741.
DR RefSeq; NP_767111.1; NC_004463.1.
DR RefSeq; WP_011083302.1; NZ_CP011360.1.
DR PDB; 1KNG; X-ray; 1.14 A; A=39-194.
DR PDBsum; 1KNG; -.
DR AlphaFoldDB; P30960; -.
DR SMR; P30960; -.
DR STRING; 224911.27348719; -.
DR EnsemblBacteria; BAC45736; BAC45736; BAC45736.
DR GeneID; 64020330; -.
DR KEGG; bja:blr0471; -.
DR PATRIC; fig|224911.44.peg.9004; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_0_5; -.
DR InParanoid; P30960; -.
DR OMA; MIGKPFP; -.
DR PhylomeDB; P30960; -.
DR EvolutionaryTrace; P30960; -.
DR Proteomes; UP000002526; 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 1: Evidence at protein level;
KW 3D-structure; Cytochrome c-type biogenesis; Disulfide bond; Periplasm;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..194
FT /note="Thiol:disulfide interchange protein CycY"
FT /id="PRO_0000034287"
FT DOMAIN 46..190
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 92..95
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:12121652"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1KNG"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1KNG"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1KNG"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1KNG"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:1KNG"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1KNG"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:1KNG"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1KNG"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:1KNG"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:1KNG"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:1KNG"
SQ SEQUENCE 194 AA; 21126 MW; 826A75D22AA0C593 CRC64;
MSEQSTSANP QRRTFLMVLP LIAFIGLALL FWFRLGSGDP SRIPSALIGR PAPQTALPPL
EGLQADNVQV PGLDPAAFKG KVSLVNVWAS WCVPCHDEAP LLTELGKDKR FQLVGINYKD
AADNARRFLG RYGNPFGRVG VDANGRASIE WGVYGVPETF VVGREGTIVY KLVGPITPDN
LRSVLLPQME KALK
