ID A0A060NIQ0_9BURK Unreviewed; 195 AA.
AC A0A060NIQ0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=SRAA_2152 {ECO:0000313|EMBL:BAO82006.1};
OS Serpentinimonas raichei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO82006.1, ECO:0000313|Proteomes:UP000067461};
RN [1] {ECO:0000313|EMBL:BAO82006.1, ECO:0000313|Proteomes:UP000067461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:BAO82006.1,
RC ECO:0000313|Proteomes:UP000067461};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|PIRNR:PIRNR001488}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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; AP014568; BAO82006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060NIQ0; -.
DR STRING; 1458425.SRAA_2152; -.
DR KEGG; cbaa:SRAA_2152; -.
DR HOGENOM; CLU_088255_1_0_4; -.
DR Proteomes; UP000067461; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd03019; DsbA_DsbA; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR023205; DsbA/DsbL.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW Isomerase {ECO:0000313|EMBL:BAO82006.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|PIRNR:PIRNR001488};
KW Reference proteome {ECO:0000313|Proteomes:UP000067461}.
FT DOMAIN 1..190
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 46..49
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 195 AA; 21970 MW; AEF78E987056601F CRC64;
MPLGAQTPAA APAFREGTHY RRLRQPAPVD APAGRIEVLE FFAYTCIHCH HFVPVFKAWK
RTVPADVVVR HVPVGFAPEF EPLQRLFYTL EAMGRLDSHH ERVFQAIHGT QRQRLHNAET
IAQWAASAGL DRARFTQTYN SFAVVSRVRR ATQLQDAYQV EGTPALGIAG RFYIPGQAER
TVQVANMLIA RVRRG
//
