ID   DKSA_BUCBP              Reviewed;         151 AA.
AC   Q89AR3;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=RNA polymerase-binding transcription factor DksA {ECO:0000255|HAMAP-Rule:MF_00926};
GN   Name=dksA {ECO:0000255|HAMAP-Rule:MF_00926}; OrderedLocusNames=bbp_184;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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:0000255|HAMAP-Rule:MF_00926}.
CC   -!- SUBUNIT: Interacts directly with the RNA polymerase.
CC       {ECO:0000255|HAMAP-Rule:MF_00926}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00926}.
CC   -!- SIMILARITY: Belongs to the DksA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00926}.
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DR   EMBL; AE016826; AAO26916.1; -; Genomic_DNA.
DR   RefSeq; WP_011091317.1; NC_004545.1.
DR   AlphaFoldDB; Q89AR3; -.
DR   SMR; Q89AR3; -.
DR   STRING; 224915.bbp_184; -.
DR   EnsemblBacteria; AAO26916; AAO26916; bbp_184.
DR   GeneID; 56470726; -.
DR   KEGG; bab:bbp_184; -.
DR   eggNOG; COG1734; Bacteria.
DR   HOGENOM; CLU_043144_2_0_6; -.
DR   OMA; KKGEEYM; -.
DR   OrthoDB; 1932026at2; -.
DR   Proteomes; UP000000601; 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   HAMAP; MF_00926; DksA; 1.
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   Pfam; PF01258; zf-dskA_traR; 1.
DR   SUPFAM; SSF109635; SSF109635; 1.
DR   TIGRFAMs; TIGR02420; dksA; 1.
DR   PROSITE; PS01102; ZF_DKSA_1; 1.
DR   PROSITE; PS51128; ZF_DKSA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..151
FT                   /note="RNA polymerase-binding transcription factor DksA"
FT                   /id="PRO_0000187544"
FT   ZN_FING         114..138
FT                   /note="dksA C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00926"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00926"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00926"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00926"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00926"
SQ   SEQUENCE   151 AA;  17876 MW;  77B443C75CD958FA CRC64;
     MQKEKNKKQS SLSILFMAGV QPYKNKKNEK YMNTKQIDHF KKILIAWKNQ LRNDISQTRL
     NIQDKATNYP DPIDRAVQEE EFSFELRHRD RERKLIEKIE KTLKKVENKD FGYCESCGIE
     IGIKRLEARP TANLCIDCKT LSEIREKQIL G