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Database: UniProt
Entry: A0A3M6QHT2_9BURK
LinkDB: A0A3M6QHT2_9BURK
Original site: A0A3M6QHT2_9BURK 
ID   A0A3M6QHT2_9BURK        Unreviewed;       164 AA.
AC   A0A3M6QHT2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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   ECO:0000313|EMBL:RMX02019.1};
GN   ORFNames=EBQ25_01920 {ECO:0000313|EMBL:RMX02019.1};
OS   Allofranklinella schreckenbergeri.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Allofranklinella.
OX   NCBI_TaxID=1076744 {ECO:0000313|EMBL:RMX02019.1, ECO:0000313|Proteomes:UP000267035};
RN   [1] {ECO:0000313|EMBL:RMX02019.1, ECO:0000313|Proteomes:UP000267035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML161473 {ECO:0000313|EMBL:RMX02019.1,
RC   ECO:0000313|Proteomes:UP000267035};
RA   Bernier A.-M., Bernard K.;
RT   "Comamonadaceae CDC group NO-1 genome sequencing and assembly.";
RL   Submitted (OCT-2018) 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:RMX02019.1}.
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DR   EMBL; RDQL01000002; RMX02019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6QHT2; -.
DR   Proteomes; UP000267035; 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:UP000267035};
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          49..119
FT                   /note="DnaK suppressor protein DksA N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21157"
FT   DOMAIN          122..156
FT                   /note="Zinc finger DksA/TraR C4-type"
FT                   /evidence="ECO:0000259|Pfam:PF01258"
FT   ZN_FING         127..151
FT                   /note="dksA C4-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   164 AA;  18324 MW;  235EE70B11BE93FE CRC64;
     MATKSAAAPT KTVAKASKAT SKSKPLDVTS LTDQDVLAMP EDDYMNDVQM AFFRHRLVAL
     KEDMLRKAGA TTEYLREEVS VVPDPADRAT IEEEHALELR TRDRERKLLK KIEQSIASID
     AGDYGYCEET GEPIGLPRLL ARPTATLSLE AQQRREIRQK MFGA
//
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