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Database: UniProt
Entry: F2K1X9_MARM1
LinkDB: F2K1X9_MARM1
Original site: F2K1X9_MARM1 
ID   F2K1X9_MARM1            Unreviewed;       235 AA.
AC   F2K1X9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   25-APR-2018, entry version 39.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   OrderedLocusNames=Marme_0690 {ECO:0000313|EMBL:ADZ89973.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028
OS   / MMB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ89973.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Lucas-Elio P., Johnston A.W.B., Sanchez-Amat A., Woyke T.;
RT   "Complete sequence of Marinomonas mediterranea MMB-1.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
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DR   EMBL; CP002583; ADZ89973.1; -; Genomic_DNA.
DR   RefSeq; WP_013659878.1; NC_015276.1.
DR   ProteinModelPortal; F2K1X9; -.
DR   STRING; 717774.Marme_0690; -.
DR   EnsemblBacteria; ADZ89973; ADZ89973; Marme_0690.
DR   KEGG; mme:Marme_0690; -.
DR   PATRIC; fig|717774.3.peg.716; -.
DR   eggNOG; ENOG4105T95; Bacteria.
DR   eggNOG; COG1651; LUCA.
DR   KO; K03981; -.
DR   OMA; QMIVYKA; -.
DR   OrthoDB; POG091H04JN; -.
DR   BioCyc; MMED717774:G1GSA-698-MONOMER; -.
DR   Proteomes; UP000001062; 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   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   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001062};
KW   Isomerase {ECO:0000313|EMBL:ADZ89973.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001062};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     23       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        24    235       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010005778.
FT   DOMAIN       29     82       DsbC_N. {ECO:0000259|Pfam:PF10411}.
FT   DOMAIN      110    233       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   235 AA;  25847 MW;  AA779D84766B31BD CRC64;
     MKIRYIFGLL TLSLTLLAQS AFAGQEEIEK ALQKAIPGAK IGSISEHSSA GLYVVSIENG
     PTLHVTKDGK YFVLGDLYRV EDSGLVNETE NAKMAKVEAM PEDQMIVFKA KDEKAHITVF
     TDVDCGYCRM LHREVDQLND LGITVRYMAY PRAGIGSPAY NTMVSIWCSD NPKYWMTQAK
     QGEEVPQNKC ENPVADQFNL GNSVGVRGTP SIVLSNGKFM PGYIEANRLA AELGL
//
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