ID A0A3F2UZJ2_9GAMM Unreviewed; 234 AA.
AC A0A3F2UZJ2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Thiol:disulfide interchange protein DsbA {ECO:0000256|ARBA:ARBA00013831};
GN ORFNames=D6160_17965 {ECO:0000313|EMBL:RLP53013.1};
OS Ketobacter sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP53013.1, ECO:0000313|Proteomes:UP000280615};
RN [1] {ECO:0000313|EMBL:RLP53013.1, ECO:0000313|Proteomes:UP000280615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BinD {ECO:0000313|EMBL:RLP53013.1};
RA Xu J.;
RT "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT genus Ketobacter and the trajectory of genomic evolution within the
RT Alcanivoraceae family.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:RLP53013.1}.
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DR EMBL; RAHY01000021; RLP53013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F2UZJ2; -.
DR Proteomes; UP000280615; 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 Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000280615}.
FT DOMAIN 45..233
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 86..89
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 234 AA; 26309 MW; 6D4D66030D60019A CRC64;
MLASDTTSRL GAGKFTLSGS RLKRDKKMKL VKQVFSLVML AGMVLSLSSQ AQAFSMERFV
EGVHYKKIEK APRQEKTVVE YFSYGCPHCN HLEPVLEAWL TDMPEGITFK RVPAIWNKSF
YVLAQLYYSL AEVGKEKELT PKVFDYLHTQ KKTIPGEAEA LQFAGDLGVD TNAFDKAWKS
EQVKQNLIKA SEEFVVHQVK GVPAIVVNGQ YQTSVSMAGS NEELFDVVEF LLNK
//
