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Database: UniProt
Entry: A0A378UKL5_BERDE
LinkDB: A0A378UKL5_BERDE
Original site: A0A378UKL5_BERDE 
ID   A0A378UKL5_BERDE        Unreviewed;       138 AA.
AC   A0A378UKL5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, 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:STZ77189.1};
GN   ORFNames=NCTC10295_01997 {ECO:0000313|EMBL:STZ77189.1};
OS   Bergeriella denitrificans (Neisseria denitrificans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Bergeriella.
OX   NCBI_TaxID=494 {ECO:0000313|EMBL:STZ77189.1, ECO:0000313|Proteomes:UP000254651};
RN   [1] {ECO:0000313|EMBL:STZ77189.1, ECO:0000313|Proteomes:UP000254651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10295 {ECO:0000313|EMBL:STZ77189.1,
RC   ECO:0000313|Proteomes:UP000254651};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-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}.
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DR   EMBL; UGQS01000002; STZ77189.1; -; Genomic_DNA.
DR   RefSeq; WP_066080516.1; NZ_UGQS01000002.1.
DR   AlphaFoldDB; A0A378UKL5; -.
DR   Proteomes; UP000254651; 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:UP000254651};
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          25..93
FT                   /note="DnaK suppressor protein DksA N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21157"
FT   DOMAIN          96..131
FT                   /note="Zinc finger DksA/TraR C4-type"
FT                   /evidence="ECO:0000259|Pfam:PF01258"
FT   ZN_FING         101..125
FT                   /note="dksA C4-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
SQ   SEQUENCE   138 AA;  15994 MW;  B5DCB9164941C084 CRC64;
     MAKLTEQDIL QWNGPEDDYM NADHLAFFRD LLVKMQEELI ENATMTAGHL QEHESAPDPA
     DRATQEEEYA LELRTRDRER KLLAKVQATI RRIDEGDYGY CDDTGEPIGL KRLLARPTAT
     LSVEAQERRE RMKKQFAD
//
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