ID Q4K907_PSEF5 Unreviewed; 255 AA.
AC Q4K907;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=dsbG {ECO:0000313|EMBL:AAY93440.1};
GN OrderedLocusNames=PFL_4184 {ECO:0000313|EMBL:AAY93440.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY93440.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY93440.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY93440.1; -; Genomic_DNA.
DR RefSeq; WP_011062459.1; NC_004129.6.
DR AlphaFoldDB; Q4K907; -.
DR STRING; 220664.PFL_4184; -.
DR GeneID; 57477248; -.
DR KEGG; pfl:PFL_4184; -.
DR PATRIC; fig|220664.5.peg.4281; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_080090_0_0_6; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF4; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBG; 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 Isomerase {ECO:0000313|EMBL:AAY93440.1};
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..24
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 25..255
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010006096"
FT DOMAIN 121..252
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 255 AA; 27733 MW; 687A80E040FB93D4 CRC64;
MPFIRHLLSL SLGAALLNAP LLQAEELPAP IRKIEEKGAK IIGSFDAPDG LKGYAAQYQN
RGMTLYLTPD GKHVLLGNLY DADGKDLSAE PLQKLVYAPM AKEVWGNLEK SNWIADGKAD
APRIVYLFSD PNCPYCNMFW EQARPWVKAG KVQLRHIMVG IIREDSPGKS AALLAAKDPQ
QALQDHEKAG KGSALKPLAS IPAAVQAKLD ANMKLMEELE LSATPAIFYL DDKGELQQQQ
GAPAPGKLTQ ILGPK
//
