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Database: UniProt
Entry: N9QDU4_9GAMM
LinkDB: N9QDU4_9GAMM
Original site: N9QDU4_9GAMM 
ID   N9QDU4_9GAMM            Unreviewed;       269 AA.
AC   N9QDU4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=F893_00423 {ECO:0000313|EMBL:ENX25052.1};
OS   Acinetobacter sp. CIP 102136.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144665 {ECO:0000313|EMBL:ENX25052.1, ECO:0000313|Proteomes:UP000013199};
RN   [1] {ECO:0000313|EMBL:ENX25052.1, ECO:0000313|Proteomes:UP000013199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102136 {ECO:0000313|EMBL:ENX25052.1,
RC   ECO:0000313|Proteomes:UP000013199};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 102136.";
RL   Submitted (FEB-2013) 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:ENX25052.1}.
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DR   EMBL; APRV01000020; ENX25052.1; -; Genomic_DNA.
DR   RefSeq; WP_005249691.1; NZ_KB850140.1.
DR   AlphaFoldDB; N9QDU4; -.
DR   PATRIC; fig|1144665.3.peg.384; -.
DR   HOGENOM; CLU_083593_0_0_6; -.
DR   Proteomes; UP000013199; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..22
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT   CHAIN           23..269
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT                   /id="PRO_5010001740"
FT   DOMAIN          63..115
FT                   /note="Disulphide bond isomerase DsbC/G N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10411"
FT   DOMAIN          147..267
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
FT   REGION          29..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  29446 MW;  3DD9E300170C1771 CRC64;
     MTFARSKIFM ACTLAAGLGL TACSNSTNND KKQELTASAP ATGEASTLTE RNAEQRLAST
     LEKHFKTAGI SAKITDIKAT EVPNLYWVSL EGMSAVYVTS DGKYLIQGDV IRLGDKQLHN
     VSENLQAGIN NKLFAELKPA DLLVYPAKGK AKHVVYVFTD VSCPYCHKFH EQMDEMNAKG
     IEVRYIAWPR GEQHMPAMEA IWCSADRRSA FDQAIAGAQI SAEKCENPVQ DQYQMGLNMG
     VNGTPAIYNS AGTYLGGYMS TSELLNRLK
//
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