ID S2L5J2_HALAF Unreviewed; 210 AA.
AC S2L5J2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=L861_07755 {ECO:0000313|EMBL:EPC00051.1};
OS Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1121939 {ECO:0000313|EMBL:EPC00051.1, ECO:0000313|Proteomes:UP000014463};
RN [1] {ECO:0000313|EMBL:EPC00051.1, ECO:0000313|Proteomes:UP000014463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35
RC {ECO:0000313|Proteomes:UP000014463};
RX PubMed=23868129; DOI=10.1128/genomeA.00497-13;
RA Tahrioui A., Quesada E., Llamas I.;
RT "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT Halomonas anticariensis FP35.";
RL Genome Announc. 1:31-31(2013).
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:EPC00051.1}.
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DR EMBL; ASTJ01000044; EPC00051.1; -; Genomic_DNA.
DR RefSeq; WP_016418988.1; NZ_KE332396.1.
DR AlphaFoldDB; S2L5J2; -.
DR STRING; 1121939.L861_07755; -.
DR PATRIC; fig|1121939.11.peg.4488; -.
DR eggNOG; COG2761; Bacteria.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000014463; 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 Reference proteome {ECO:0000313|Proteomes:UP000014463};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..210
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004510361"
FT DOMAIN 8..152
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 210 AA; 23100 MW; 7C6C523FF79946E3 CRC64;
MFKTLVAVLA GLSLSTLASA QSLVEGEQYK VLDEAVPTQV EEGQIEVVEA FWYGCPHCYS
LEDPLNAWVA ELPEDVTFRR MPATMGGDWN KHAVAFYAAQ ELGILEDVHD DFFDAVHQEG
RHLTEVDDIA DFFSDYGVSE DEARQALTSF GVKSQVNQAH ARMRAYGLMG VPALIVEGRY
VITPSSAGSL ENMPQIASAL IEKVRDDGNQ
//
