ID S9RZN3_9RHOB Unreviewed; 180 AA.
AC S9RZN3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Cytochrome c-type biogenesis protein CcmG/DsbE, thiol:disulfide oxidoreductase {ECO:0000313|EMBL:EPX79444.1};
GN ORFNames=thalar_02269 {ECO:0000313|EMBL:EPX79444.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79444.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000256|ARBA:ARBA00007758}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPX79444.1}.
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DR EMBL; AONI01000010; EPX79444.1; -; Genomic_DNA.
DR RefSeq; WP_021100824.1; NZ_KE557306.1.
DR AlphaFoldDB; S9RZN3; -.
DR STRING; 1123360.thalar_02269; -.
DR PATRIC; fig|1123360.3.peg.2246; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_0_5; -.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000015351; Unassembled WGS sequence.
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 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 Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000015351}.
FT DOMAIN 36..180
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 180 AA; 19267 MW; DFF52EF2221BAB93 CRC64;
MKRVLFALPL LVALIIGGFA IWGLSGGRDP SSIPSVLISQ PVPQLALEPI AGVDTPGLTT
EDFSKIEGIK LLNVFASWCA PCRAEHPILT RMAQEEGLTL VGINYKDKPE AAAKWLAELG
NPYEAIGSDY SGRAGIDLGI SGVPETFIID EDGIIRHRFA GPVVGDGLTR FTEALDEVRK
//
