ID A8APA0_CITK8 Unreviewed; 237 AA.
AC A8APA0;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN OrderedLocusNames=CKO_04255 {ECO:0000313|EMBL:ABV15313.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV15313.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV15313.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-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}.
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DR EMBL; CP000822; ABV15313.1; -; Genomic_DNA.
DR RefSeq; WP_012134997.1; NC_009792.1.
DR AlphaFoldDB; A8APA0; -.
DR STRING; 290338.CKO_04255; -.
DR GeneID; 45137858; -.
DR KEGG; cko:CKO_04255; -.
DR HOGENOM; CLU_083593_0_0_6; -.
DR OMA; QMIVYKA; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000008148; 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 InterPro; IPR017937; Thioredoxin_CS.
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.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000008148};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 22..237
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010006679"
FT DOMAIN 27..76
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 104..227
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 237 AA; 25932 MW; 1F20B49DCB510DEF CRC64;
MKKRFMMFTL LAAAFSGMVH ADDAAIRQSL TKLGVQSTEI QPAPVAGMKT VLTNSGVLYV
TDDGKHIIQG PMYDVSGASP VNVTNQLLMK HLNALEKEMI VYKAPQEKHV ITIFTDITCG
YCHKLHEEMK DYNALGITVR YLAFPRQGLE SQAEQDMKSI WCAKDRNKAF DEAMAGKGVK
AATCDIDIAN HYALGVQFGV SGTPAIVLSN GYVVPGYQGP KEMKAFLDAH QKQTSGK
//