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Database: UniProt
Entry: A0A1G5Q2Z7_9RHOB
LinkDB: A0A1G5Q2Z7_9RHOB
Original site: A0A1G5Q2Z7_9RHOB 
ID   A0A1G5Q2Z7_9RHOB        Unreviewed;       180 AA.
AC   A0A1G5Q2Z7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Cytochrome c biogenesis protein CcmG, thiol:disulfide interchange protein DsbE {ECO:0000313|EMBL:SCZ55830.1};
GN   ORFNames=SAMN04488118_102482 {ECO:0000313|EMBL:SCZ55830.1};
OS   Epibacterium ulvae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Epibacterium.
OX   NCBI_TaxID=1156985 {ECO:0000313|EMBL:SCZ55830.1, ECO:0000313|Proteomes:UP000198767};
RN   [1] {ECO:0000313|EMBL:SCZ55830.1, ECO:0000313|Proteomes:UP000198767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U95 {ECO:0000313|EMBL:SCZ55830.1,
RC   ECO:0000313|Proteomes:UP000198767};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC       {ECO:0000256|ARBA:ARBA00007758}.
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DR   EMBL; FMWG01000002; SCZ55830.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5Q2Z7; -.
DR   STRING; 1156985.SAMN04488118_102482; -.
DR   OrthoDB; 9799347at2; -.
DR   Proteomes; UP000198767; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   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 {ECO:0000256|ARBA:ARBA00022748};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198767};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..173
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   180 AA;  19616 MW;  927F2618D4385040 CRC64;
     MVKVSPLMAV PVALFTGFAM LAFVGLHRDD PDGLPSVLVG RDAPAVSSAP LLEYPEFQTA
     DLQGQGISLV NFWASWCAPC RAEHPNLMEL AETYPVYGIN QDYGEKDAKA FLDELGNPYA
     GILFDGSKRQ SIDWGVYGLP ETFVVDEDGK ILARIAGPLT QRVIENTLEP IFAAQVSEKQ
//
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