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Database: UniProt
Entry: F8GG98_NITSI
LinkDB: F8GG98_NITSI
Original site: F8GG98_NITSI 
ID   F8GG98_NITSI            Unreviewed;       212 AA.
AC   F8GG98;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN   OrderedLocusNames=Nit79A3_2605 {ECO:0000313|EMBL:AEJ02372.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ02372.1};
RN   [1] {ECO:0000313|EMBL:AEJ02372.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ02372.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA   Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|PIRNR:PIRNR001488}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
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DR   EMBL; CP002876; AEJ02372.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8GG98; -.
DR   STRING; 261292.Nit79A3_2605; -.
DR   KEGG; nii:Nit79A3_2605; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_1_0_4; -.
DR   OrthoDB; 9784896at2; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|PIRNR:PIRNR001488};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..212
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003371580"
FT   DOMAIN          12..206
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        59..62
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   212 AA;  24220 MW;  2FAF2BC6C0893B95 CRC64;
     MNQYKPLAVF FLLLSFSLIS LSSARADIVE GKDYTVLATP QPTQDGNTIE VLEFFWYGCP
     HCDSLHPHLK TWLMNIPKDV SFRYVPATLR ANWVAAAKIF YTIEAIGKTD VLHDKVYDAV
     HRDKIDINNE SVLFDWVEKQ GIDRKKFEDT YRSFSVQNQV ARSTQLSRQY QLTGVPALVI
     NGKYITSGKM GGTPQDTIRT LEALIEKIRK EK
//
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