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Database: UniProt
Entry: A0A0G3XBY2_9SPHN
LinkDB: A0A0G3XBY2_9SPHN
Original site: A0A0G3XBY2_9SPHN 
ID   A0A0G3XBY2_9SPHN        Unreviewed;       152 AA.
AC   A0A0G3XBY2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=AM2010_2037 {ECO:0000313|EMBL:AKM08099.1};
OS   Pelagerythrobacter marensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Pelagerythrobacter.
OX   NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM08099.1, ECO:0000313|Proteomes:UP000037643};
RN   [1] {ECO:0000313|EMBL:AKM08099.1, ECO:0000313|Proteomes:UP000037643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM08099.1,
RC   ECO:0000313|Proteomes:UP000037643};
RA   Kim K.M.;
RL   Submitted (JUN-2015) 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; CP011805; AKM08099.1; -; Genomic_DNA.
DR   RefSeq; WP_047806983.1; NZ_LMVG01000004.1.
DR   AlphaFoldDB; A0A0G3XBY2; -.
DR   STRING; 543877.AM2010_2037; -.
DR   KEGG; amx:AM2010_2037; -.
DR   PATRIC; fig|543877.4.peg.2069; -.
DR   OrthoDB; 9803742at2; -.
DR   Proteomes; UP000037643; 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_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:UP000037643};
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          36..106
FT                   /note="DnaK suppressor protein DksA N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21157"
FT   DOMAIN          109..144
FT                   /note="Zinc finger DksA/TraR C4-type"
FT                   /evidence="ECO:0000259|Pfam:PF01258"
FT   ZN_FING         114..138
FT                   /note="dksA C4-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   152 AA;  17431 MW;  FCDB90EE04154DD4 CRC64;
     MASATSTDIE VLEKARQSIA PDYEPSDDEP YMNEQQTNFF RMLLLEWKRS ILSASSATLQ
     SLQDGPIREP DLNDRASSET DWSIELRTRD RQRKLIAKID SALRRIDDGE YGYCEVTGDP
     IGLRRLIARP VATMTVEAQE AHERREKISR DD
//
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