DKSA_ECOL6
ID DKSA_ECOL6 Reviewed; 151 AA.
AC P0ABS2; P18274;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=c0178;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN78672.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN78672.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001155227.1; NC_004431.1.
DR AlphaFoldDB; P0ABS2; -.
DR SMR; P0ABS2; -.
DR STRING; 199310.c0178; -.
DR EnsemblBacteria; AAN78672; AAN78672; c0178.
DR GeneID; 60371850; -.
DR GeneID; 67416218; -.
DR KEGG; ecc:c0178; -.
DR eggNOG; COG1734; Bacteria.
DR HOGENOM; CLU_043144_2_0_6; -.
DR OMA; KKGEEYM; -.
DR Proteomes; UP000001410; 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; IPR020460; Znf_C4-type_bac.
DR InterPro; IPR000962; Znf_DskA_TraR.
DR InterPro; IPR020458; Znf_DskA_TraR_CS.
DR Pfam; PF01258; zf-dskA_traR; 1.
DR PRINTS; PR00618; DKSAZNFINGER.
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 Coiled coil; Cytoplasm; Metal-binding; Zinc; Zinc-finger.
FT CHAIN 1..151
FT /note="RNA polymerase-binding transcription factor DksA"
FT /id="PRO_0000187538"
FT ZN_FING 114..138
FT /note="dksA C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00926"
FT COILED 33..54
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; 17528 MW; 620842DB15E066A9 CRC64;
MQEGQNRKTS SLSILAIAGV EPYQEKPGEE YMNEAQLAHF RRILEAWRNQ LRDEVDRTVT
HMQDEAANFP DPVDRAAQEE EFSLELRNRD RERKLIKKIE KTLKKVEDED FGYCESCGVE
IGIRRLEARP TADLCIDCKT LAEIREKQMA G