ID A0A367M3H9_PSEAI Unreviewed; 163 AA. AC A0A367M3H9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-NOV-2019, entry version 6. DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038}; DE Flags: Fragment; GN ORFNames=DT376_26505 {ECO:0000313|EMBL:RCI71919.1}; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287 {ECO:0000313|EMBL:RCI71919.1, ECO:0000313|Proteomes:UP000253594}; RN [1] {ECO:0000313|EMBL:RCI71919.1, ECO:0000313|Proteomes:UP000253594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B2-305 {ECO:0000313|EMBL:RCI71919.1, RC ECO:0000313|Proteomes:UP000253594}; RA Ballaben A.S., Darini A.L.C., Doi Y.; RT "Mechanisms of high-level aminoglycoside resistance among Gram- RT negative pathogens in Brazil."; RL Submitted (JUL-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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RCI71919.1}. 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; QORE01001166; RCI71919.1; -; Genomic_DNA. DR Proteomes; UP000253594; Unassembled WGS sequence. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. 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; 3.40.30.10; -; 1. DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR Pfam; PF13098; Thioredoxin_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000253594}; KW Isomerase {ECO:0000313|EMBL:RCI71919.1}; KW Periplasm {ECO:0000256|RuleBase:RU364038}; KW Redox-active center {ECO:0000256|RuleBase:RU364038}; KW Signal {ECO:0000256|RuleBase:RU364038}. FT DOMAIN 7 163 Thioredoxin. {ECO:0000259|PROSITE: FT PS51352}. FT NON_TER 1 1 {ECO:0000313|EMBL:RCI71919.1}. SQ SEQUENCE 163 AA; 17555 MW; E745A7BB2568A3A2 CRC64; VKDGKPVNLT EKAESQAIAK AINGVPASEM VVYPAKGQAK AHITVFTDTT CPYCQKLHAE VPDLTEQGIE VRYMAFPRQG PQSAGDKQLQ AVWCAKEPTK AMDAMMNGKE IKSSECKNPV DKQFQMGQMV GVQGTPAIVL ANGQLLPGYQ PAKQLAKLAL EAK //