ID A0A0P9CQF2_9GAMM Unreviewed; 144 AA.
AC A0A0P9CQF2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=SAMN05661077_1710 {ECO:0000313|EMBL:SCY28624.1};
OS Thiohalorhabdus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalorhabdales;
OC Thiohalorhabdaceae; Thiohalorhabdus.
OX NCBI_TaxID=381306 {ECO:0000313|EMBL:SCY28624.1, ECO:0000313|Proteomes:UP000183104};
RN [1] {ECO:0000313|Proteomes:UP000183104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL 19 {ECO:0000313|Proteomes:UP000183104};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00926}.
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DR EMBL; FMUN01000004; SCY28624.1; -; Genomic_DNA.
DR RefSeq; WP_054965052.1; NZ_LJCP01000006.1.
DR AlphaFoldDB; A0A0P9CQF2; -.
DR STRING; 381306.AN478_02550; -.
DR PATRIC; fig|381306.5.peg.2078; -.
DR OrthoDB; 9803742at2; -.
DR Proteomes; UP000183104; Unassembled WGS sequence.
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 InterPro; IPR020458; Znf_DskA_TraR_CS.
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; PS01102; ZF_DKSA_1; 1.
DR PROSITE; PS51128; ZF_DKSA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000183104};
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 29..98
FT /note="DnaK suppressor protein DksA N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21157"
FT DOMAIN 101..136
FT /note="Zinc finger DksA/TraR C4-type"
FT /evidence="ECO:0000259|Pfam:PF01258"
FT ZN_FING 106..130
FT /note="dksA C4-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 144 AA; 17029 MW; 573C380F5AB32698 CRC64;
MTEKVDLDEI ELEPDYRPSP DEPYMNPKQL AFFRRKLLDW RNQIVEDTTH TRQNMNESEN
QADEVDRASQ ETERYTELRT VEREQRLLSK IDAALRRIEN GEFGYCEVTG EPIGVRRLEA
RPVATLSIEA KEAQERQERQ MAED
//
