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Database: UniProt
Entry: Q2IVP2_RHOP2
LinkDB: Q2IVP2_RHOP2
Original site: Q2IVP2_RHOP2 
ID   Q2IVP2_RHOP2            Unreviewed;       255 AA.
AC   Q2IVP2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=DSBA oxidoreductase {ECO:0000313|EMBL:ABD07718.1};
GN   OrderedLocusNames=RPB_3016 {ECO:0000313|EMBL:ABD07718.1};
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD07718.1, ECO:0000313|Proteomes:UP000008809};
RN   [1] {ECO:0000313|EMBL:ABD07718.1, ECO:0000313|Proteomes:UP000008809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2 {ECO:0000313|EMBL:ABD07718.1,
RC   ECO:0000313|Proteomes:UP000008809};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000250; ABD07718.1; -; Genomic_DNA.
DR   RefSeq; WP_011441902.1; NC_007778.1.
DR   AlphaFoldDB; Q2IVP2; -.
DR   STRING; 316058.RPB_3016; -.
DR   KEGG; rpb:RPB_3016; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_000288_47_4_5; -.
DR   OrthoDB; 9780147at2; -.
DR   Proteomes; UP000008809; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03023; DsbA_Com1_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR041205; ScsC_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   Pfam; PF18312; ScsC_N; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..255
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004209976"
FT   DOMAIN          56..250
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   255 AA;  27651 MW;  C8C6E3F88744AD58 CRC64;
     MPSFRPFAAA LLALLLVGAP VAAAAQKFSD EQRSQIEQII KDYLVSHPEV LEEASDELGK
     RQANAAAEKH QAAIKDNAEA IFNSPRGITL GNKDGDVTFV EFFDYNCGYC KRAMTDMIAL
     MKEDPKLKIV LKEFPVLGPP SVEAAQVAIA VRMQTPDGKK YLDFHQKLMG GRGQADKARA
     MAAAKEAGFD MARLEKDMAS PEVRATIEES FKLAEAMGMN GTPSYVIGKQ VVVGAVGLDT
     LRQKVALARC GKEKC
//
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