ID A0A1I1MZB6_9GAMM Unreviewed; 308 AA.
AC A0A1I1MZB6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=SAMN05660831_00040 {ECO:0000313|EMBL:SFC90727.1};
OS Thiohalospira halophila DSM 15071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalospirales;
OC Thiohalospiraceae; Thiohalospira.
OX NCBI_TaxID=1123397 {ECO:0000313|EMBL:SFC90727.1, ECO:0000313|Proteomes:UP000198611};
RN [1] {ECO:0000313|EMBL:SFC90727.1, ECO:0000313|Proteomes:UP000198611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL3 {ECO:0000313|EMBL:SFC90727.1,
RC ECO:0000313|Proteomes:UP000198611};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by transferring its disulfide bond to other proteins and
CC is reduced in the process. {ECO:0000256|RuleBase:RU364038}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
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DR EMBL; FOMJ01000001; SFC90727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1MZB6; -.
DR STRING; 1123397.SAMN05660831_00040; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000198611; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:SFC90727.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000198611};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT DOMAIN 180..306
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
FT REGION 35..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 32126 MW; 24875A7BF190D457 CRC64;
MNKKLVQGVS LGLVAGAVAG VLVAKNAGPM GQWVPASGAG TADSAASSPA PQDGAAPTNP
GALPAVFEGV DIGKDQVIAE FETAVPQLRG YILQRAENRV PMAVYVTPDR KHMIAGAMID
ENGDSMTAQH YQRHSGYTKD ELAALANNQG SSDKGGSPAG STEEVLAGLK DATLVTQGSG
GAEMYVLMDV DCPYCKRLYH TVSSLRDEVT VNWVMVGYRG PRAQQTAAKI LGHDDPASAL
DQVMADRQAL ADYEGATAME AVEENTEAAQ KLGLRGTPHG VVLPADGGEA QRLRGAAPES
RLRQMMGL
//