ID   DKSA_BUCAP              Reviewed;         151 AA.
AC   Q8K9U5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BUsg_192;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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       Also required for regulation of fis expression. {ECO:0000255|HAMAP-
CC       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; AE013218; AAM67757.1; -; Genomic_DNA.
DR   RefSeq; WP_011053724.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9U5; -.
DR   SMR; Q8K9U5; -.
DR   STRING; 198804.BUsg_192; -.
DR   EnsemblBacteria; AAM67757; AAM67757; BUsg_192.
DR   KEGG; bas:BUsg_192; -.
DR   eggNOG; COG1734; Bacteria.
DR   HOGENOM; CLU_043144_2_0_6; -.
DR   OMA; KKGEEYM; -.
DR   OrthoDB; 1932026at2; -.
DR   Proteomes; UP000000416; 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; Zinc; Zinc-finger.
FT   CHAIN           1..151
FT                   /note="RNA polymerase-binding transcription factor DksA"
FT                   /id="PRO_0000187543"
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;  17720 MW;  B6127A6769521EE9 CRC64;
     MEKEQNKKTS SLNVLAIAGL QPYQKKTDEE YMNEKQMLHF KKILETWKNQ LTIEINHTLL
     YIQDKSTNFP DPIDRAAQEE EFSLELRNRD RSRKLIKKIQ ETLKKIKDKD FGYCNSCAVE
     IGIRRLEARP TANLCIDCKT LAEIREKQMA G