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Database: UniProt
Entry: V5FMY0_9VIBR
LinkDB: V5FMY0_9VIBR
Original site: V5FMY0_9VIBR 
ID   V5FMY0_9VIBR            Unreviewed;       200 AA.
AC   V5FMY0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   Name=dsbA {ECO:0000313|EMBL:GAD90951.1};
GN   ORFNames=VHA01S_061_00200 {ECO:0000313|EMBL:GAD90951.1};
OS   Vibrio halioticoli NBRC 102217.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219072 {ECO:0000313|EMBL:GAD90951.1, ECO:0000313|Proteomes:UP000017800};
RN   [1] {ECO:0000313|EMBL:GAD90951.1, ECO:0000313|Proteomes:UP000017800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90951.1,
RC   ECO:0000313|Proteomes:UP000017800};
RA   Ichikawa N., Kimura A., Ohji S., Hosoyama A., Fujita N.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAD90951.1, ECO:0000313|Proteomes:UP000017800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90951.1,
RC   ECO:0000313|Proteomes:UP000017800};
RA   Isaki S., Kimura A., Ohji S., Hosoyama A., Fujita N., Hashimoto M.,
RA   Hosoyama Y., Yamazoe A.;
RT   "Whole genome shotgun sequence of Vibrio halioticoli NBRC 102217.";
RL   Submitted (NOV-2013) 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:GAD90951.1}.
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DR   EMBL; BAUJ01000061; GAD90951.1; -; Genomic_DNA.
DR   RefSeq; WP_023405255.1; NZ_BAUJ01000061.1.
DR   AlphaFoldDB; V5FMY0; -.
DR   eggNOG; COG1651; Bacteria.
DR   OrthoDB; 9784896at2; -.
DR   Proteomes; UP000017800; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|PIRNR:PIRNR001488};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..200
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004732774"
FT   DOMAIN          6..198
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   200 AA;  22368 MW;  B4B8DCAFCB80F068 CRC64;
     MKKLIALVAT MFLTLSVHAA QFTEGQNYTV LDLPASSSPT VNEFFSFYCP HCYQFEPIIK
     NLKSSLPANA KFQKSHVSFM GGSMGLSMSK AYATMVVLEV EDKMIPVMFN RIHKLNAAPR
     DEAELRQIFL DEGVDAKKFD AAFKGFAVDS MARRFDKKFK DSNLKGVPSI VINNKYLVEM
     GSVKSAKDLS DLVNYLLTLK
//
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