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Database: UniProt
Entry: A0A0F4PHD6_9GAMM
LinkDB: A0A0F4PHD6_9GAMM
Original site: A0A0F4PHD6_9GAMM 
ID   A0A0F4PHD6_9GAMM        Unreviewed;       249 AA.
AC   A0A0F4PHD6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=CWC05_18215 {ECO:0000313|EMBL:TMP85512.1}, TW72_14655
GN   {ECO:0000313|EMBL:KJY97078.1};
OS   Pseudoalteromonas ruthenica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY97078.1, ECO:0000313|Proteomes:UP000033664};
RN   [1] {ECO:0000313|EMBL:KJY97078.1, ECO:0000313|Proteomes:UP000033664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3137 {ECO:0000313|EMBL:KJY97078.1,
RC   ECO:0000313|Proteomes:UP000033664};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
RN   [2] {ECO:0000313|EMBL:TMP85512.1, ECO:0000313|Proteomes:UP000305874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2897 {ECO:0000313|EMBL:TMP85512.1,
RC   ECO:0000313|Proteomes:UP000305874};
RA   Paulsen S., Gram L.K.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000305874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2897 {ECO:0000313|Proteomes:UP000305874};
RA   Sonnenschein E.C., Bech P.K.;
RT   "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT   Pseudoalteromonas.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:TMP85512.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S2897 {ECO:0000313|EMBL:TMP85512.1};
RA   Sonnenschein E.C., Bech P.K.;
RT   "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT   Pseudoalteromonas.";
RL   Submitted (SEP-2019) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJY97078.1}.
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DR   EMBL; JXXZ01000013; KJY97078.1; -; Genomic_DNA.
DR   EMBL; PNCG01000025; TMP85512.1; -; Genomic_DNA.
DR   RefSeq; WP_022943331.1; NZ_PPSV01000016.1.
DR   AlphaFoldDB; A0A0F4PHD6; -.
DR   STRING; 151081.TW72_14655; -.
DR   GeneID; 58229737; -.
DR   PATRIC; fig|151081.8.peg.3767; -.
DR   eggNOG; COG1651; Bacteria.
DR   OrthoDB; 12976at2; -.
DR   Proteomes; UP000033664; Unassembled WGS sequence.
DR   Proteomes; UP000305874; Unassembled WGS sequence.
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   InterPro; IPR017937; Thioredoxin_CS.
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.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:TMP85512.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033664};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT   CHAIN           20..249
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT                   /id="PRO_5034013146"
FT   DOMAIN          39..89
FT                   /note="Disulphide bond isomerase DsbC/G N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10411"
FT   DOMAIN          117..239
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
SQ   SEQUENCE   249 AA;  26836 MW;  373CF25BC5AE5869 CRC64;
     MKKLVVALAF AGASAGAFAQ GVSVEPQDTM QQQVSVIQSK LAELGVNVKQ VHPSPVQGLQ
     EVITDKGVFY ASADGRYLVQ GTMIDLVNRE NLTESALSHV RLEGVAQYQN SMITYKADNE
     KGKITVFTDI TCGYCRKLHR ELDDYLDAGI TVQYLAFPRG GLRGSGYTDL MNVWCADNKQ
     EALTEAKAGE KPEKIENCNA PVAEHYQLGQ SFGISGTPAI ILSDGSMIPG YQPAAAISSA
     IDELNNNKS
//
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