ID A0A0N0E5U5_9PSED Unreviewed; 243 AA.
AC A0A0N0E5U5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
DE Flags: Precursor;
GN ORFNames=PF66_00646 {ECO:0000313|EMBL:KPA92905.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA92905.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA92905.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA92905.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(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:KPA92905.1}.
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DR EMBL; JSYZ01000002; KPA92905.1; -; Genomic_DNA.
DR RefSeq; WP_054059193.1; NZ_JTBY01000145.1.
DR AlphaFoldDB; A0A0N0E5U5; -.
DR STRING; 50340.PF66_00646; -.
DR PATRIC; fig|50340.43.peg.2653; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000037931; 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; 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 Isomerase {ECO:0000313|EMBL:KPA92905.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 22..243
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010004654"
FT DOMAIN 30..83
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 116..238
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 243 AA; 25932 MW; DD1DEA986114F661 CRC64;
MRLIQIFAAA ALALASTFAL ADDAAEQAIR KSLDSLQLET PVESITASPL SGLYEVKLKG
SRVLYASADG QFVMQGYLFQ LKDGKPVNLT EKTERLGISK LINGIPVAET VVYPAIGETK
SHITVFTDTT CPYCHKLHAE VPALNKMGIE VRYVAFPRQG LGSPGDQQLQ AVWCSTDKRA
AMDKMVEGEE IKAAKCTNPV SRQFALGQSI GVNGTPAIVL ADGQVIPGYQ PAAQVAKLAL
AAK
//