ID Q5K698_NEIGO Unreviewed; 239 AA.
AC Q5K698;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=dsbC {ECO:0000313|EMBL:AAW83067.1};
GN Synonyms=dsbC_1 {ECO:0000313|EMBL:SBM87513.1};
GN ORFNames=WHOF_00182 {ECO:0000313|EMBL:SBM87513.1}, WHOF_00857
GN {ECO:0000313|EMBL:SBQ20106.1};
OS Neisseria gonorrhoeae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485 {ECO:0000313|EMBL:AAQ03232.1};
RN [1] {ECO:0000313|EMBL:AAQ03232.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2005 {ECO:0000313|EMBL:AAQ03232.1};
RA Urvil P.T., Hart A., Nguyen K., Das M., Kurosky A., Smith J., Nowicki B.J.,
RA Nowicki S.;
RT "A pathogenicity island from PID isolate of Neisseria gonorrhoeae.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAW83067.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MS11 {ECO:0000313|EMBL:AAW83067.1};
RX PubMed=15752195; DOI=10.1111/j.1365-2958.2005.04521.x;
RA Hamilton H.L., Dominguez N.M., Schwartz K.J., Hackett K.T., Dillard J.P.;
RT "Neisseria gonorrhoeae secretes chromosomal DNA via a novel type IV
RT secretion system.";
RL Mol. Microbiol. 55:1704-1721(2005).
RN [3] {ECO:0000313|EMBL:SBM87513.1, ECO:0000313|Proteomes:UP000239837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHO F {ECO:0000313|EMBL:SBM87513.1,
RC ECO:0000313|Proteomes:UP000239837};
RG Pathogen Informatics;
RL Submitted (MAY-2016) 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; AF411857; AAQ03232.1; -; Genomic_DNA.
DR EMBL; AY803022; AAW83067.1; -; Genomic_DNA.
DR EMBL; FLKW01000001; SBM87513.1; -; Genomic_DNA.
DR EMBL; LT591897; SBQ20106.1; -; Genomic_DNA.
DR RefSeq; WP_003693119.1; NZ_VCDH01000011.1.
DR TCDB; 3.A.7.11.1; the type iv (conjugal dna-protein transfer or virb) secretory pathway (ivsp) family.
DR PATRIC; fig|485.41.peg.24; -.
DR Proteomes; UP000239837; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 21..239
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5014486719"
FT DOMAIN 28..78
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 112..233
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 239 AA; 26673 MW; 8958E94D933143CB CRC64;
MKKKILATIA AITAFQTAFA DVKTVGSTLH KLYPNTTFSS VKATPMASIY EVTMGDNIAY
VQENGRYFIF GALYDMQEQK DLTEMARSAV TQKSYSRLPF KNAIKIVKGN GGKGKREFAL
FSDPDCPFCR RLEETLAGMT DYTAYVFMFP IKSLHPDAIS KAEHIWCSKD REKAWNNYML
MDKEPAAGNC KNPVSENIAL AEQLKVRGTP SMIHKDGRRT SGAMPRAELE KWLNGAGAE
//
