ID A0A2S1JUV0_9GAMM Unreviewed; 249 AA.
AC A0A2S1JUV0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=BTJ40_15780 {ECO:0000313|EMBL:AWF82172.1};
OS Microbulbifer sp. A4B17.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=359370 {ECO:0000313|EMBL:AWF82172.1, ECO:0000313|Proteomes:UP000244764};
RN [1] {ECO:0000313|EMBL:AWF82172.1, ECO:0000313|Proteomes:UP000244764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4B17 {ECO:0000313|EMBL:AWF82172.1,
RC ECO:0000313|Proteomes:UP000244764};
RX PubMed=16885309; DOI=10.1128/AEM.00494-06;
RA Peng X., Adachi K., Chen C., Kasai H., Kanoh K., Shizuri Y., Misawa N.;
RT "Discovery of a marine bacterium producing 4-hydroxybenzoate and its alkyl
RT esters, parabens.";
RL Appl. Environ. Microbiol. 72:5556-5561(2006).
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; CP029064; AWF82172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1JUV0; -.
DR KEGG; mii:BTJ40_15780; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000244764; 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; 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 Isomerase {ECO:0000313|EMBL:AWF82172.1};
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..249
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5015372864"
FT DOMAIN 35..89
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 122..247
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 249 AA; 27122 MW; 939ECA606E0A09C8 CRC64;
MTLIKKPLAI AGALLSLVGS AALAEVDTNV VKTIKTRLEA SNPKATYGEV RESPIEGLYE
VDVDDGNTTL FVSADGNHFV YGDLYQVKAG GVANLSEQRR ATRRAEVMGA LDTEDMIVFS
PKGETKASVY VFTDVDCGYC RKLHQDVPEL NKRGIEVRYL AFPRGGLNSL GYRKLATAWC
AEDSNKTLTA LKNRENVPLD VCKTNPVAAQ YKLGNEAIDV RGTPTIVMED GRVVPGYLPP
DRLLKELGI
//
