ID A0A1V1PUY1_9PROT Unreviewed; 137 AA.
AC A0A1V1PUY1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=U91I_03923 {ECO:0000313|EMBL:GAN00258.1};
OS alpha proteobacterium U9-1i.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1605283 {ECO:0000313|EMBL:GAN00258.1, ECO:0000313|Proteomes:UP000188260};
RN [1] {ECO:0000313|EMBL:GAN00258.1, ECO:0000313|Proteomes:UP000188260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U9-1i {ECO:0000313|EMBL:GAN00258.1,
RC ECO:0000313|Proteomes:UP000188260};
RA Okano K., Furuta S., Ichise S., Miyata N.;
RT "Whole-Genome Sequences of Two Manganese(II)-Oxidizing Bacteria, Bosea sp.
RT Strain BIWAKO-01 and Alphaproteobacterium Strain U9-1i.";
RL Genome Announc. 4:e01309-16(2016).
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:GAN00258.1}.
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DR EMBL; BBSY01000004; GAN00258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1PUY1; -.
DR STRING; 1605283.U91I_03923; -.
DR OrthoDB; 9803742at2; -.
DR Proteomes; UP000188260; 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:UP000188260};
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 21..91
FT /note="DnaK suppressor protein DksA N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21157"
FT DOMAIN 94..129
FT /note="Zinc finger DksA/TraR C4-type"
FT /evidence="ECO:0000259|Pfam:PF01258"
FT ZN_FING 99..123
FT /note="dksA C4-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
SQ SEQUENCE 137 AA; 16079 MW; 9B6FC88E7AD52227 CRC64;
MAVKTTEYRP SDKEPFMNER QRDYFRKKLL AWKDEIIEES RATIAALQQD TVAEPDIADR
ASSETDRATE LRTRDRQRKL ISKIDDAIRR IDDGSYGYCE ETGEPIALSR LEARPIATLS
LEAQERHERR ERVHRDD
//
