ID A1SZS5_PSYIN Unreviewed; 251 AA.
AC A1SZS5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN OrderedLocusNames=Ping_3303 {ECO:0000313|EMBL:ABM04990.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM04990.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM04990.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM04990.1,
RC ECO:0000313|Proteomes:UP000000639};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) 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; CP000510; ABM04990.1; -; Genomic_DNA.
DR RefSeq; WP_011771542.1; NC_008709.1.
DR AlphaFoldDB; A1SZS5; -.
DR STRING; 357804.Ping_3303; -.
DR KEGG; pin:Ping_3303; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_0_0_6; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000000639; Chromosome.
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:UP000000639};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 24..251
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010001117"
FT DOMAIN 45..88
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 125..248
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 251 AA; 28034 MW; D14125CA2586152F CRC64;
MATIFSKTGV ICVFLLSSFA AVSATSESPS SLVVEEITTK MESLKIPVNE INKSAVEGLY
EVISNGDIYY ISEDATHLLY GSIYALDNQM VNITEQKKAQ LSRQKVAKNI DKITAFEKDM
IVFKAQDEKH VVTVFTDPTC SYCQKLHSQM ADYNKLGITI RYLAFPRAGI DSSTYHTMVS
IWCSNDPKNA MNMAKKRREI PSETCENTVK EQYQLGRLLG VNGTPALILE NGTLTPGYLP
PQRLLQLLEE K
//
