ID V2GMI8_9BURK Unreviewed; 228 AA.
AC V2GMI8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=B551_0222075 {ECO:0000313|EMBL:ESH91326.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESH91326.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESH91326.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) 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 {ECO:0000256|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESH91326.1}.
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DR EMBL; AMPR02000441; ESH91326.1; -; Genomic_DNA.
DR AlphaFoldDB; V2GMI8; -.
DR Proteomes; UP000053474; 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:UP000053474};
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 114..183
FT /note="DnaK suppressor protein DksA N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21157"
FT DOMAIN 186..220
FT /note="Zinc finger DksA/TraR C4-type"
FT /evidence="ECO:0000259|Pfam:PF01258"
FT ZN_FING 191..215
FT /note="dksA C4-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 24889 MW; 6D8C2C5689D562BD CRC64;
MVAAAKTKES RSKTAGAAAA TTKAQGQQAA PTPRNGSAPA GTGAAKGGTR SSKTAASQSE
TVEPRKRTDT ASARNTTPPV ASTRESAATM SSNKLLTEAE ILKMDDKDYM NEAQLAFFKN
RLEQLRDEIL KNADQTTEHL RETVIVPDPA DRATIEEEHA LELRTRDRER KLLKKVEQSL
ARIESGDYGW CEETGEPIGV PRLLARPTAT LSLEAQQRRE LRQKLFGD
//
