ID T1PWP9_SALEN Unreviewed; 356 AA.
AC T1PWP9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=trbB {ECO:0000313|EMBL:AFR24457.1};
GN ORFNames=GJG57_23020 {ECO:0000313|EMBL:HAB3400393.1};
OS Salmonella enteritidis.
OG Plasmid pS1400_89 {ECO:0000313|EMBL:AFR24457.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=149539 {ECO:0000313|EMBL:AFR24457.1};
RN [1] {ECO:0000313|EMBL:AFR24457.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S1400/94 {ECO:0000313|EMBL:AFR24457.1};
RC PLASMID=pS1400_89 {ECO:0000313|EMBL:AFR24457.1};
RA Coward C., Sait L., Cogan T., Humphrey T.J., Maskell D.J.;
RT "Acquisition of an 89kb plasmid in Salmonella enterica Enteritidis confers
RT increased invasiveness and promotes the growth of SE in eggs.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAB3400393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ILBSalm5516484 {ECO:0000313|EMBL:HAB3400393.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:HAB3400393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ILBSalm5516484 {ECO:0000313|EMBL:HAB3400393.1};
RG NCBI Pathogen Detection Project;
RL Submitted (FEB-2019) 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|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|RuleBase:RU364038}.
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DR EMBL; JN796410; AFR24457.1; -; Genomic_DNA.
DR EMBL; DAAGKE010000022; HAB3400393.1; -; Genomic_DNA.
DR RefSeq; WP_021013257.1; NC_022267.1.
DR RefSeq; YP_008520322.1; NC_022267.1.
DR AlphaFoldDB; T1PWP9; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Periplasm {ECO:0000256|RuleBase:RU364038};
KW Plasmid {ECO:0000313|EMBL:AFR24457.1};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|RuleBase:RU364038};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 97..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 356 AA; 39579 MW; C351C4A0BA10651F CRC64;
MTIEYFATRI AKHISVQAIW PDGRTEIIAV LPRDALSGLV TRNNQLIHIA FDAMGTRNRE
TVLIDKQEHN ADQILTAIDS CLRLEYLMER RFSRTPLFRA IIASVVLFVM ATIAVFLFRY
VDRVFWDDTT PEAVQTAGEP RLLPPHLNHT VPLNEGIQLP VPPKKDVQVP EKTITGKNPE
AAAARHNLAT VLKRNADRGM FTINLSSGHE RTLFAFLDPA CPNCRLLEPA LKRLASDFNV
VIYPVSVIGG EESTDRVAPL LCEKDAQKRA AGWHRLYSAD NGMMTPSEET TPADETCLKA
ARAAIDVNNV AFRKFGFAGT PWVLSDTGWH LPTGILQETG TLNLFLKTTD SESGHE
//
