ID A0A058ZQ45_9RHOB Unreviewed; 250 AA.
AC A0A058ZQ45;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=DSBA oxidoreductase {ECO:0000313|EMBL:KCV83365.1};
GN ORFNames=ATO10_01350 {ECO:0000313|EMBL:KCV83365.1};
OS Actibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1461693 {ECO:0000313|EMBL:KCV83365.1, ECO:0000313|Proteomes:UP000024836};
RN [1] {ECO:0000313|EMBL:KCV83365.1, ECO:0000313|Proteomes:UP000024836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-Z10 {ECO:0000313|Proteomes:UP000024836};
RA Lai Q., Li G., Shao Z.;
RT "Shimia sp. 22II-S11-Z10 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for disulfide bond formation in some
CC proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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:KCV83365.1}.
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; AQQY01000001; KCV83365.1; -; Genomic_DNA.
DR RefSeq; WP_035247023.1; NZ_AQQY01000001.1.
DR AlphaFoldDB; A0A058ZQ45; -.
DR STRING; 1461693.ATO10_01350; -.
DR PATRIC; fig|1461693.3.peg.282; -.
DR eggNOG; COG1651; Bacteria.
DR OrthoDB; 9780147at2; -.
DR Proteomes; UP000024836; Unassembled WGS sequence.
DR CDD; cd03023; DsbA_Com1_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR041205; ScsC_N.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF5; THIOREDOXIN-LIKE_FOLD DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF18312; ScsC_N; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000024836};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..250
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001566868"
FT DOMAIN 57..249
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 250 AA; 27260 MW; F40EB4622F1E1301 CRC64;
MIRQMISGAA LSLGLMASSA FATDLSALSQ AEREAFRAEV RAYLLENPEV LMEAIAVLED
RQASQQTVAD VALVIENAEA LFNDGYSWVG GNPEGDITIV EFTDYRCGYC RKAHDEVAEL
IKSDGNIRFI VKEFPILGEA SDLSSRFAIA TKLVEGADAY KKAHDALIKF RGNVSVESLA
KLGDKMGFDT DEVMAVMLSA QVDDEINANR ALAQRMQIAG TPTFVVKETL LRGYVPLEGM
RQVVAQSRAN
//
