ID A0A3N6NW16_9CYAN Unreviewed; 261 AA.
AC A0A3N6NW16;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Disulfide bond formation protein DsbA {ECO:0000313|EMBL:RQH40869.1};
GN ORFNames=D5R40_15925 {ECO:0000313|EMBL:RQH40869.1};
OS Okeania hirsuta.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Okeania.
OX NCBI_TaxID=1458930 {ECO:0000313|EMBL:RQH40869.1, ECO:0000313|Proteomes:UP000269154};
RN [1] {ECO:0000313|EMBL:RQH40869.1, ECO:0000313|Proteomes:UP000269154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAB10Feb10-1 {ECO:0000313|EMBL:RQH40869.1,
RC ECO:0000313|Proteomes:UP000269154};
RX PubMed=30444349;
RA Moss N.A., Leao T., Rankin M., McCullough T.M., Qu P., Korobeynikov A.,
RA Smith J.L., Gerwick L., Gerwick W.H.;
RT "Ketoreductase domain dysfunction expands chemodiversity: malyngamide
RT biosynthesis in the cyanobacterium Okeania hirsuta.";
RL ACS Chem. Biol. 0:0-0(2018).
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:RQH40869.1}.
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; RCBY01000084; RQH40869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6NW16; -.
DR OrthoDB; 117402at2; -.
DR Proteomes; UP000269154; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000269154};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..261
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 261 AA; 29646 MW; F54C202CEFBC489D CRC64;
MSNFSTRFNL YNLKVLYFIA IFSIVIAISG CTPSAQSTGT QVNSEELEQQ VLQIIRNNPE
AIIESVQAYQ QQQQEQQQAS KQEVLKQFKT NPQAKIGNSP TFGSTEQKIV LFEFSDFQCP
FCSKVQVNLK EFMDKHQDRV TLVFKHLPLV RIHPQAIPAA KASWAAQQQG KFWEYHDALF
EQQDKLGEEF YIEIANNLNL DIEKFNSDRK SQEATDSIQQ DFQLAQEIGA SGTPFFVMNG
ETFSGAVKVS DMEKLLAKVS Q
//
