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Database: UniProt
Entry: C7NHG6_KYTSD
LinkDB: C7NHG6_KYTSD
Original site: C7NHG6_KYTSD 
ID   C7NHG6_KYTSD            Unreviewed;       276 AA.
AC   C7NHG6;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:ACV06323.1};
GN   OrderedLocusNames=Ksed_12910 {ECO:0000313|EMBL:ACV06323.1};
OS   Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS   (Micrococcus sedentarius).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC   Kytococcus.
OX   NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06323.1, ECO:0000313|Proteomes:UP000006666};
RN   [1] {ECO:0000313|EMBL:ACV06323.1, ECO:0000313|Proteomes:UP000006666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC   {ECO:0000313|Proteomes:UP000006666};
RX   PubMed=21304632; DOI=10.4056/sigs.761;
RA   Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA   Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL   Stand. Genomic Sci. 1:12-20(2009).
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DR   EMBL; CP001686; ACV06323.1; -; Genomic_DNA.
DR   RefSeq; WP_015779268.1; NC_013169.1.
DR   AlphaFoldDB; C7NHG6; -.
DR   STRING; 478801.Ksed_12910; -.
DR   KEGG; kse:Ksed_12910; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_000288_47_3_11; -.
DR   Proteomes; UP000006666; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd02972; DsbA_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR13887:SF56; THIOREDOXIN-LIKE REDUCTASE RV2466C; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:ACV06323.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..261
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13462"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  28605 MW;  59ED4B31926BD3B6 CRC64;
     MPVDNSPRPS GAHRPAGSSG GGVSKALIAL IAALVVGALV VLGIWLLGQG DDDDSTAAPS
     SSTNSQSGSG DPSSGTPADM AVPQGMPEKP AGVTVGEAGG PELIIFEDFQ CPACKSFEDL
     LGDDIATMID DGKAQVTYFP KTFLDGNLGT DHSERAASAA FCASDGGKFR EYHDALFANH
     PEREGDGWTD EQLKGFGKDA GLEGDALATF EKCVADGTYR EYAKASEARS SEMGVMSTPT
     VYLNGQRMEL TNAEDFRKQV DEAGAPQKSD ASPSAS
//
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