ID A0A2P8KKE2_9BURK Unreviewed; 214 AA.
AC A0A2P8KKE2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=C7T35_16290 {ECO:0000313|EMBL:PSL83446.1}, GXN78_09660
GN {ECO:0000313|EMBL:NDZ13126.1};
OS Variovorax sp. WS11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL83446.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL83446.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL83446.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDZ13126.1, ECO:0000313|Proteomes:UP000479786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:NDZ13126.1,
RC ECO:0000313|Proteomes:UP000479786};
RA Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT WS11.";
RL Submitted (FEB-2020) 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:PSL83446.1}.
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DR EMBL; JAAGOW010000001; NDZ13126.1; -; Genomic_DNA.
DR EMBL; PXZZ01000020; PSL83446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8KKE2; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR Proteomes; UP000479786; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..214
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033765604"
FT DOMAIN 16..170
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 61..64
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 214 AA; 23948 MW; 21E6DC12DFCFCE56 CRC64;
MKRRDFSLAA TSLGLLPLMT PTHAQTLGPK AGTDYAVLDK RVPVDAPAGK VEVIEFFWYN
CPHCNAFEPT LEAWIKKLPP HVAFKRVPVA FQASFQPQQK LYYALEAMGK VDEYQLKVFN
AIHQQRQNLS GEQQIIDWVA ANGLDKAKFT EQYKSFSVAS KIQRAKQLQD AYQVAGVPSI
GIAGRWYVDG DLAKSMERAL QVTDFLIGEA RKSA
//
