ID   A0A380UF67_ACIHA        Unreviewed;       217 AA.
AC   A0A380UF67;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   16-JAN-2019, entry version 3.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbC_2 {ECO:0000313|EMBL:SUU08023.1};
GN   ORFNames=NCTC10306_00774 {ECO:0000313|EMBL:SUU08023.1};
OS   Acinetobacter haemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=29430 {ECO:0000313|EMBL:SUU08023.1, ECO:0000313|Proteomes:UP000255161};
RN   [1] {ECO:0000313|EMBL:SUU08023.1, ECO:0000313|Proteomes:UP000255161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10306 {ECO:0000313|EMBL:SUU08023.1,
RC   ECO:0000313|Proteomes:UP000255161};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
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DR   EMBL; UFRT01000001; SUU08023.1; -; Genomic_DNA.
DR   Proteomes; UP000255161; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 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   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000255161};
KW   Isomerase {ECO:0000313|EMBL:SUU08023.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   DOMAIN       77    217       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   217 AA;  24407 MW;  623101E2DF6E32DA CRC64;
     MMSLANVETL KSNLNKNYPD IQVTNIQATE MTGLYSANLD NQIIYLDENA EHMFIGSMVR
     LKDQKNLTKD LVLKQNSIDW QKLPLQDAIK TVKGNGKRQL AIFSDPNCPY CKQLEAELDK
     LNDVTIYTFI YALKPQSIAV SKQVWCDANP SYAWKNLLQK NVQPKAKTCA NPIDRNLALG
     RKLGVNGTPT LIFSNGLKMV GGRSAEDIQM IWKELGL
//