ID A0A2T3MSY4_9GAMM Unreviewed; 201 AA.
AC A0A2T3MSY4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=C9I89_20035 {ECO:0000313|EMBL:PSW01421.1};
OS Photobacterium lipolyticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=266810 {ECO:0000313|EMBL:PSW01421.1, ECO:0000313|Proteomes:UP000240904};
RN [1] {ECO:0000313|EMBL:PSW01421.1, ECO:0000313|Proteomes:UP000240904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16190 {ECO:0000313|EMBL:PSW01421.1,
RC ECO:0000313|Proteomes:UP000240904};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:PSW01421.1}.
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; PYMC01000021; PSW01421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3MSY4; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000240904; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
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; IPR017937; Thioredoxin_CS.
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; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|PIRNR:PIRNR001488};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000240904};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..201
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015492171"
FT DOMAIN 7..200
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 50..53
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 201 AA; 22374 MW; 3F0290D72D32BB93 CRC64;
MMKKLLALAS AALLSFSVHA AKFTEGEHYK VLELPKSSNP IVTEFFSFYC PHCSRFEPII
QALKKNLPDN AKLQKNHVSF MGGPMGNSMS KAYSTAVVMG VDDKMIPVLF NRVHTMKKPP
RNDQELRQIF IDEGMSAEDF DGAYNSFAVN SMVNRANKLF TDSGLTGVPA VIVNNKYLVQ
AGGKIKSTEE YVELVNFLLK K
//
