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Database: UniProt
Entry: K0NNT1_DESTT
LinkDB: K0NNT1_DESTT
Original site: K0NNT1_DESTT 
ID   K0NNT1_DESTT            Unreviewed;       290 AA.
AC   K0NNT1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Tetratricopeptide repeat protein {ECO:0000313|EMBL:CCK80427.1};
GN   OrderedLocusNames=TOL2_C22660 {ECO:0000313|EMBL:CCK80427.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80427.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK80427.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
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DR   EMBL; FO203503; CCK80427.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0NNT1; -.
DR   STRING; 651182.TOL2_C22660; -.
DR   KEGG; dto:TOL2_C22660; -.
DR   PATRIC; fig|651182.5.peg.2680; -.
DR   HOGENOM; CLU_003728_0_0_7; -.
DR   OMA; GYFLILQ; -.
DR   Proteomes; UP000007347; Chromosome.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44835:SF1; PROTEIN O-GLCNAC TRANSFERASE; 1.
DR   PANTHER; PTHR44835; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REPEAT          109..142
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          143..176
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          177..210
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          241..274
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   290 AA;  33168 MW;  179F8237F38BC700 CRC64;
     MVEPRVTYGN PSQDHIRDIP QVRYKALSES IENKQLPEIN ADEYEKLGDA LLSKGKYFMA
     YMQYENSLKK NKDNIRVEYK KGAALLGGGR NEEAQKIFKL ILQKQPDFAL AHEGMGRVNF
     KNKSYHIAKL NFEKAVDLNP LLWRSYAYLG NLYDFKKDYD LAVKEYKTAL TIKPDAGYIH
     NNMGASLYMS GRYKNAVDSF YQALRSNYNS KKVYNNLGRA FVALELYDNA LEAFEKGGTK
     ASAYNNIGVG YLKNGNTTKA AECFEKAIEL SPRFYVLANE NLKKCRLKQQ
//
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