ID A0A090AQ78_9GAMM Unreviewed; 142 AA.
AC A0A090AQ78;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=RNA polymerase-binding transcription factor DksA {ECO:0000256|HAMAP-Rule:MF_00926};
GN Name=dksA {ECO:0000256|HAMAP-Rule:MF_00926};
GN ORFNames=THII_3473 {ECO:0000313|EMBL:BAP57770.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP57770.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP57770.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
CC -!- FUNCTION: Transcription factor that acts by binding directly to the RNA
CC polymerase (RNAP). Required for negative regulation of rRNA expression
CC and positive regulation of several amino acid biosynthesis promoters.
CC Also required for regulation of fis expression. {ECO:0000256|HAMAP-
CC Rule:MF_00926}.
CC -!- SUBUNIT: Interacts directly with the RNA polymerase.
CC {ECO:0000256|HAMAP-Rule:MF_00926}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}.
CC -!- SIMILARITY: Belongs to the DksA family. {ECO:0000256|HAMAP-
CC Rule:MF_00926}.
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DR EMBL; AP014633; BAP57770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AQ78; -.
DR STRING; 40754.THII_3473; -.
DR KEGG; tig:THII_3473; -.
DR HOGENOM; CLU_043144_2_0_6; -.
DR OrthoDB; 9803742at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.910; DksA, coiled-coil domain; 1.
DR HAMAP; MF_00926; DksA; 1.
DR InterPro; IPR048489; DksA_N.
DR InterPro; IPR012784; DksA_RNA_pol-bd.
DR InterPro; IPR037187; DnaK_N.
DR InterPro; IPR000962; Znf_DskA_TraR.
DR NCBIfam; TIGR02420; dksA; 1.
DR PANTHER; PTHR33823:SF2; RNA POLYMERASE-BINDING TRANSCRIPTION FACTOR DKSA; 1.
DR PANTHER; PTHR33823; RNA POLYMERASE-BINDING TRANSCRIPTION FACTOR DKSA-RELATED; 1.
DR Pfam; PF21157; DksA_CC; 1.
DR Pfam; PF01258; zf-dskA_traR; 1.
DR SUPFAM; SSF109635; DnaK suppressor protein DksA, alpha-hairpin domain; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51128; ZF_DKSA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00926}; Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00926};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00926}.
FT DOMAIN 27..97
FT /note="DnaK suppressor protein DksA N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21157"
FT DOMAIN 100..134
FT /note="Zinc finger DksA/TraR C4-type"
FT /evidence="ECO:0000259|Pfam:PF01258"
FT ZN_FING 105..129
FT /note="dksA C4-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00926"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00926"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00926"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00926"
SQ SEQUENCE 142 AA; 16928 MW; ACE14BAA9FCB1A55 CRC64;
MSEIKMNELN FTPYQLRPGE EYMNDQQLEH FRQILLQWKE QLIAEVKRTR HHMQDEAVNF
ADLNDRATQE EEFTLELRAR DRERKLIKKI DEALKGIEVG EYGFCETCGI EVGLRRLEAR
PTATKCVDCQ ERHEIQERQT FG
//
