ID U3G9F9_9RALS Unreviewed; 248 AA.
AC U3G9F9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=HMPREF0989_03722 {ECO:0000313|EMBL:EGY62167.1};
OS Ralstonia sp. 5_2_56FAA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=658080 {ECO:0000313|EMBL:EGY62167.1, ECO:0000313|Proteomes:UP000016506};
RN [1] {ECO:0000313|EMBL:EGY62167.1, ECO:0000313|Proteomes:UP000016506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5_2_56FAA {ECO:0000313|EMBL:EGY62167.1,
RC ECO:0000313|Proteomes:UP000016506};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Daigneault M.,
RA Ambrose C.E., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Ralstonia sp. 5_2_56FAA.";
RL Submitted (MAY-2012) 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 -!- 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:EGY62167.1}.
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DR EMBL; ACTT02000017; EGY62167.1; -; Genomic_DNA.
DR RefSeq; WP_009241994.1; NZ_JH815240.1.
DR AlphaFoldDB; U3G9F9; -.
DR GeneID; 61391460; -.
DR PATRIC; fig|402626.5.peg.4272; -.
DR HOGENOM; CLU_083593_1_1_4; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000016506; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 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.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000016506};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 30..248
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010000274"
FT DOMAIN 43..91
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 120..240
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 248 AA; 26581 MW; DA2BAB1BE8446EE1 CRC64;
MSFRIRVAAI ASAVAVAAIG AGYVLSAGAA EPALDKVKAT VQKALGPNVE IKSVTKSPLA
GLYEINLGSQ VVYSDATGRY VLNGDLLDTQ TATNLTQERL AELNRVKWSD LPLDRAVKWV
KGNGARKIAV FSDPNCPYCH KLEQMLTQVD NVTVYTFLFP ILSEDSNTKA KQIWCSADRA
KAWRDWMTAK TAPGGAGTCD TPLEANLKLG QQLNVTGTPA IIFPDGSRAP GLIDAATLER
KFAALKKS
//