ID A0A380UF67_ACIHA Unreviewed; 217 AA. AC A0A380UF67; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 24-JAN-2024, entry version 15. 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; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC 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 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; UFRT01000001; SUU08023.1; -; Genomic_DNA. DR AlphaFoldDB; A0A380UF67; -. DR Proteomes; UP000255161; Unassembled WGS sequence. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt. 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 InterPro; IPR013766; Thioredoxin_domain. 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. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000313|EMBL:SUU08023.1}; 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 DOMAIN 77..217 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE: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 //