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Database: UniProt
Entry: A0A5C0B8A7_9BURK
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ID   A0A5C0B8A7_9BURK        Unreviewed;       119 AA.
AC   A0A5C0B8A7;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   02-APR-2025, entry version 13.
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:QEI09077.1};
GN   ORFNames=FXN63_02550 {ECO:0000313|EMBL:QEI09077.1};
OS   Pigmentiphaga aceris.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Pigmentiphaga.
OX   NCBI_TaxID=1940612 {ECO:0000313|EMBL:QEI09077.1, ECO:0000313|Proteomes:UP000325161};
RN   [1] {ECO:0000313|EMBL:QEI09077.1, ECO:0000313|Proteomes:UP000325161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mada1488 {ECO:0000313|EMBL:QEI09077.1,
RC   ECO:0000313|Proteomes:UP000325161};
RA   Bletz M.C., Bunk B., Sproeer C., Biwer P., Reiter S., Rabemananjara F.C.E.,
RA   Schulz S., Overmann J., Vences M.;
RT   "Amphibian skin-associated Pigmentiphaga: genome sequence and occurrence
RT   across geography and hosts.";
RL   Submitted (AUG-2019) 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}.
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DR   EMBL; CP043046; QEI09077.1; -; Genomic_DNA.
DR   RefSeq; WP_148818850.1; NZ_CP043046.1.
DR   AlphaFoldDB; A0A5C0B8A7; -.
DR   KEGG; pacr:FXN63_02550; -.
DR   OrthoDB; 9803742at2; -.
DR   Proteomes; UP000325161; 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   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_N; 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:UP000325161};
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          5..74
FT                   /note="DnaK suppressor protein DksA N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21157"
FT   DOMAIN          77..111
FT                   /note="Zinc finger DksA/TraR C4-type"
FT                   /evidence="ECO:0000259|Pfam:PF01258"
FT   ZN_FING         82..106
FT                   /note="dksA C4-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
SQ   SEQUENCE   119 AA;  13840 MW;  4284BCEEF7759919 CRC64;
     MSERQLAFFR NRLHEIEREL LSNAGETTEH LRETAFVPDP ADRATIEEEH ALELRTRDRE
     RKLLKKVQQS LARIDGGDYG WCEETGEPIG IPRLLARPTA TLSLEAQQRR ELRQKLYGD
//
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