ID A0A0G3XNL8_9SPHN Unreviewed; 300 AA.
AC A0A0G3XNL8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=AB433_17785 {ECO:0000313|EMBL:AKM12143.1};
OS Croceicoccus naphthovorans.
OG Plasmid p1 {ECO:0000313|EMBL:AKM12143.1,
OG ECO:0000313|Proteomes:UP000035287}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM12143.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM12143.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM12143.1,
RC ECO:0000313|Proteomes:UP000035287};
RC PLASMID=Plasmid p1 {ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-2015) 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. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
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DR EMBL; CP011771; AKM12143.1; -; Genomic_DNA.
DR RefSeq; WP_037486392.1; NZ_JACIEL010000024.1.
DR AlphaFoldDB; A0A0G3XNL8; -.
DR KEGG; cna:AB433_17785; -.
DR PATRIC; fig|1348774.3.peg.3747; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000035287; Plasmid p1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR018950; DiS-bond_isomerase_DsbC/G_N.
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; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Plasmid {ECO:0000313|EMBL:AKM12143.1};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000035287};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 40..300
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010005537"
FT DOMAIN 59..109
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 182..295
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 32163 MW; 2FF87507A76F6B7A CRC64;
MTFHFADLKR LKPTKRAVKR LAWPLAAMAL GSGASLVWAN SEGGERRPSE ADVAVASLLK
ERLPRTAVSR VNCQVVDGVC EVTAGSQLFY VDRTARYLMI GRVYDMQTRQ DLTAVRLLEV
NPDLLVGGAA GSRREAETTQ ASARGLNTSA AREASAQGAP RTMSLAQLPG AGGIVWGNPA
GKTVTVFSDF RCGYCRALSA ELEAMNVRVI ERPISVLGSR DLANQVFCAR NRPRAVKAAY
AGAPITDSKP CDTSALDANE RFAREAGIAG TPVIVRSDGA VIEGYRPRAV LETWLKAVRS
//
