ID D8JNX3_ACISD Unreviewed; 236 AA.
AC D8JNX3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN OrderedLocusNames=AOLE_03095 {ECO:0000313|EMBL:ADI89520.1};
OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI89520.1, ECO:0000313|Proteomes:UP000000392};
RN [1] {ECO:0000313|EMBL:ADI89520.1, ECO:0000313|Proteomes:UP000000392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16667 / KCTC 23045 / DR1
RC {ECO:0000313|Proteomes:UP000000392};
RX PubMed=20639327; DOI=10.1128/JB.00722-10;
RA Jung J., Baek J.H., Park W.;
RT "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT DR1.";
RL J. Bacteriol. 192:4794-4795(2010).
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; CP002080; ADI89520.1; -; Genomic_DNA.
DR RefSeq; WP_005309781.1; NZ_VEIV01000007.1.
DR AlphaFoldDB; D8JNX3; -.
DR GeneID; 9381032; -.
DR KEGG; acd:AOLE_03095; -.
DR PATRIC; fig|436717.3.peg.621; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_1_1_6; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000000392; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 21..236
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010008259"
FT DOMAIN 26..78
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 107..231
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 236 AA; 26385 MW; 1099C7C1445FC44A CRC64;
MKTKLATLML SLAIFGSAHA DVKALEQNLK TNYPDLPVKG VYQSPVQGIY EVYTSGRIVY
TNQDAKYFFV GNLVDIKQQK NMTEERIAEL GKIDVKSLPL NQAIKYVKGK GERTIYVFSD
PDCPYCQRLE QNMVGVDNVT VYVFLYPLTS LHPNAEKVSN QIWCSKNPAE AWTNYMLNRK
LPTNSKSCSS PIQKNIALGQ KLNIDGTPTL FLQDGQRLSG VPSDAKQIEA LLQSAK
//
