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Database: UniProt
Entry: I3TWK0_TISMK
LinkDB: I3TWK0_TISMK
Original site: I3TWK0_TISMK 
ID   I3TWK0_TISMK            Unreviewed;       459 AA.
AC   I3TWK0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=C4-dicarboxylate transport transcriptional regulatory protein dctD {ECO:0000313|EMBL:AFK57138.1};
GN   Name=dctD {ECO:0000313|EMBL:AFK57138.1};
GN   OrderedLocusNames=TMO_c0528 {ECO:0000313|EMBL:AFK57138.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM3 {ECO:0000313|EMBL:AFK57138.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK57138.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK57138.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK57138.1,
RC   ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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DR   EMBL; CP003239; AFK57138.1; -; Genomic_DNA.
DR   RefSeq; WP_014748127.1; NC_017958.1.
DR   AlphaFoldDB; I3TWK0; -.
DR   KEGG; tmo:TMO_c0528; -.
DR   PATRIC; fig|1110502.3.peg.5403; -.
DR   HOGENOM; CLU_000445_0_5_5; -.
DR   Proteomes; UP000005258; Plasmid pTM3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   PANTHER; PTHR32071:SF57; SIGMA L-DEPENDENT TRANSCRIPTIONAL REGULATOR YQIR-RELATED; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Plasmid {ECO:0000313|EMBL:AFK57138.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          7..121
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          145..374
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   REGION          379..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   459 AA;  50199 MW;  4AE06BC54EFCECF1 CRC64;
     MTRELPQVVF VDDEDDVRIA NAQTLDLAGF DVLTAASAEA ALALVDREFP GVVVTDMRMP
     GIDGLTLFDR LRAQDPDLPV IFVTGHGDIP MAVEAMRRGA QDFLSKPYPA EALVDAVTRA
     TRLRRLVMEN RRLKAALDAE AALGLIGRTP EMERLRETVQ AVAAADVDVL VLGETGSGKE
     VVARALHAGS RRRTARLVAL NCGALPETVI ESELFGHEPG AFTGAQRRRV GRIEHADGGT
     LFLDEIESMP KSLQVKLLRV LETRTVEPLG TNDIRPVDLR VIGATKVDLL QEAAEGRFRD
     DLYYRLNVVT IRIPPLRERR GDVPLLFAHF LERAAARFGR PVPAPDDAVR RHLAAHDWPG
     NVRELAHFAE RVALGLSAET APGSGPLPAG AAGPGDDPDL PLPRRVDRFE AGAIRAALAL
     HDGEVKAVIQ ALGLPRKTFY DKLQRHGIDP NDYRRTRRS
//
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