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
//