ID R9B8V2_9GAMM Unreviewed; 205 AA.
AC R9B8V2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=I593_00538 {ECO:0000313|EMBL:EOR10888.1};
OS Acinetobacter tandoii DSM 14970 = CIP 107469.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR10888.1, ECO:0000313|Proteomes:UP000016201};
RN [1] {ECO:0000313|EMBL:EOR10888.1, ECO:0000313|Proteomes:UP000016201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR10888.1,
RC ECO:0000313|Proteomes:UP000016201};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL Submitted (MAR-2013) 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}.
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:EOR10888.1}.
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DR EMBL; AQFM01000022; EOR10888.1; -; Genomic_DNA.
DR RefSeq; WP_016165694.1; NZ_KE007359.1.
DR AlphaFoldDB; R9B8V2; -.
DR PATRIC; fig|1120927.3.peg.510; -.
DR eggNOG; COG1651; Bacteria.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000016201; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..205
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004471125"
FT DOMAIN 22..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 205 AA; 22987 MW; 4FBC4C19A101DAA4 CRC64;
MKKFLLGSLA TAVFAFSGSV MAANFVAGKD YTVVANPGKV EVPGKIEVRE FFWYGCPHCF
KLEPHMQTWL KNIPKDVRFV RTPAAMNPVW EQGARGYYVS EALGVRQKTH LPLFHAIHVN
GQQIFDQQSQ AKFFTKYGVP EAKFNSMFNS FMITSKVAQA NQLAKQYQLT GVPAVVVNGK
YVVQGEDAKV TQVVSYLVEK ERKAK
//
