ID A0A0F4QXU2_9GAMM Unreviewed; 243 AA.
AC A0A0F4QXU2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=TW77_03135 {ECO:0000313|EMBL:KJZ12085.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ12085.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ12085.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ12085.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(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. 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:KJZ12085.1}.
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DR EMBL; JXYA01000006; KJZ12085.1; -; Genomic_DNA.
DR RefSeq; WP_046003520.1; NZ_JXYA01000006.1.
DR AlphaFoldDB; A0A0F4QXU2; -.
DR PATRIC; fig|43658.5.peg.655; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000033452; 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 InterPro; IPR017937; Thioredoxin_CS.
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.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000033452};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 19..243
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010005535"
FT DOMAIN 40..84
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 112..236
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 243 AA; 25985 MW; 00D98EA32E51111E CRC64;
MKKLLLAASL AFSVGAFAET TQEVSPMAVS PIASQFADLG LTVKSVSDSP ISGLKTVITD
KGVFYASPNG QYLVQGTMID VTNRRNITED ALSDVRKSGV AQYQDSMIVY KAENEKHQIT
VFTDITCGYC RKLHRELEDY LAAGITVKYL AFPRGGLSGN GYKSLMNVWC AEDAAAALTE
AKAGNEVPDV KNCQAPVAEH YQLGQSFGIS GTPAIVLEDG SMIPGYQPAD ALAKMLNQAS
KKS
//
