ID A0A0N9UZC9_SPHMC Unreviewed; 289 AA.
AC A0A0N9UZC9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=AN936_13045 {ECO:0000313|EMBL:ALH81256.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH81256.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH81256.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH81256.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
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; CP012700; ALH81256.1; -; Genomic_DNA.
DR RefSeq; WP_054588505.1; NZ_CP013344.1.
DR AlphaFoldDB; A0A0N9UZC9; -.
DR KEGG; smag:AN936_13045; -.
DR PATRIC; fig|33050.5.peg.2694; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000058074; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 43..289
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010004655"
FT DOMAIN 50..102
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 164..279
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 289 AA; 30566 MW; 8EE6C6F0CC2E56E4 CRC64;
MNFNEFRPGL KARVAHLSLA AASAAALLTS GVAVVTAMPA QAAIARDVAQ ALKLRLPKTP
IDALDCTTFA PWCEVVSGES LFYIDEAARY LFVGRLYDLE ERRDVTAARL LELNPDLLAA
GAARAAGRAE THSPEARTAP AKTMVDLSGL PKDGAVLWGN RRGPRLVVFS DFQCGYCQRL
TGELEAAAVL VEERPISIFG ASSRRMSEGV LCAKDKAKAL HAAYAGRAPS APANCDVGEA
LDTNEAFARA NGFAGTPVIV RASDGAVLHG YRDAATLRKF ANAKPGGRK
//
