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Database: UniProt
Entry: A0A1H6D5N6_9GAMM
LinkDB: A0A1H6D5N6_9GAMM
Original site: A0A1H6D5N6_9GAMM 
ID   A0A1H6D5N6_9GAMM        Unreviewed;       243 AA.
AC   A0A1H6D5N6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=SAMN05444390_10564 {ECO:0000313|EMBL:SEG80689.1};
OS   Marinobacterium lutimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=568106 {ECO:0000313|EMBL:SEG80689.1, ECO:0000313|Proteomes:UP000236745};
RN   [1] {ECO:0000313|EMBL:SEG80689.1, ECO:0000313|Proteomes:UP000236745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22012 {ECO:0000313|EMBL:SEG80689.1,
RC   ECO:0000313|Proteomes:UP000236745};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNVQ01000005; SEG80689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6D5N6; -.
DR   OrthoDB; 12976at2; -.
DR   Proteomes; UP000236745; 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   Reference proteome {ECO:0000313|Proteomes:UP000236745};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT   CHAIN           20..243
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT                   /id="PRO_5010000991"
FT   DOMAIN          31..81
FT                   /note="Disulphide bond isomerase DsbC/G N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10411"
FT   DOMAIN          114..241
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
SQ   SEQUENCE   243 AA;  26726 MW;  D8CCA1AF553D596B CRC64;
     MRALVAAMLM LVVAQGAQAA EDANNKIAER IKSVDSRLDV ESVTATPMDG LFEVVLSSGE
     VLYTDSEGEY VLSGELFHLE QGRGLVNLTE QRMQKVRVDA LAKIPAEQRV VFPAKGERKA
     RIQVFTDVDC VYCRRLHSEV ETLNEMGIEV DYLAFPRGGE RSAAAGKMSA IWCAEPGEER
     RELMNRAKAG EALEPVNCEN PVLDQFHLGQ QLGVNGTPAL ILDNGQMLPG YVPAERLKQI
     LEI
//
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