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Database: UniProt
Entry: A0A0N0E5U5_9PSED
LinkDB: A0A0N0E5U5_9PSED
Original site: A0A0N0E5U5_9PSED 
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
//
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