ID A0A175XYN0_9SPHN Unreviewed; 290 AA.
AC A0A175XYN0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=AVM11_11810 {ECO:0000313|EMBL:KZB93552.1};
OS Sphingomonas melonis TY.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=621456 {ECO:0000313|EMBL:KZB93552.1, ECO:0000313|Proteomes:UP000078460};
RN [1] {ECO:0000313|EMBL:KZB93552.1, ECO:0000313|Proteomes:UP000078460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY {ECO:0000313|EMBL:KZB93552.1,
RC ECO:0000313|Proteomes:UP000078460};
RA Wang H., Zhu P.;
RT "Sphingomonas melonis TY, whole genome shotgun sequencing.";
RL Submitted (MAR-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. 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}.
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:KZB93552.1}.
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DR EMBL; LQCK02000068; KZB93552.1; -; Genomic_DNA.
DR RefSeq; WP_062126118.1; NZ_LQCK02000068.1.
DR AlphaFoldDB; A0A175XYN0; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000078460; Unassembled WGS sequence.
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 Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 35..290
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010002136"
FT DOMAIN 50..102
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 168..284
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
FT REGION 122..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 30627 MW; D989F3768E5487C8 CRC64;
MSATDYLAFW RLRPRFLATV AACSAVVGFG AAGAASTLGL MSTSDAKVEA LLKARLPKTQ
VTKINCAIVE GLCEVTAGSN LFYVDRSGRY LMIGRVYDME TRQDLTATRL LEINPDTLIG
GAAKANNAPS SDEAPLTRGA GAPPPAPAAP QHLSLTSLPA TGAIVWGKSG GKTVTVFSDF
RCGYCRALSN TLRTMNVRVV ERPISVLGSR DLANQVYCAK NREEALHQAY AGEPLRNAGT
CDTSGLDANE KFARAHGLSG TPVIVRSDGA MIEGYRPKEA LAAFIEGGRS
//
