ID A0A3D9BSM8_9RHOB Unreviewed; 140 AA.
AC A0A3D9BSM8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
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:REC56530.1};
GN ORFNames=DRV84_09320 {ECO:0000313|EMBL:REC56530.1};
OS Rhodosalinus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC56530.1, ECO:0000313|Proteomes:UP000257131};
RN [1] {ECO:0000313|EMBL:REC56530.1, ECO:0000313|Proteomes:UP000257131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDN1C137 {ECO:0000313|EMBL:REC56530.1,
RC ECO:0000313|Proteomes:UP000257131};
RX PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT saltern.";
RL Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REC56530.1}.
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DR EMBL; QOHR01000011; REC56530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9BSM8; -.
DR OrthoDB; 9803742at2; -.
DR Proteomes; UP000257131; 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:UP000257131};
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 24..94
FT /note="DnaK suppressor protein DksA N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21157"
FT DOMAIN 97..132
FT /note="Zinc finger DksA/TraR C4-type"
FT /evidence="ECO:0000259|Pfam:PF01258"
FT ZN_FING 102..126
FT /note="dksA C4-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00510"
SQ SEQUENCE 140 AA; 16517 MW; 781059B6B86B8786 CRC64;
MKAETFLPED YRPAEDEPFM NERQLEYFRR KLLAWKAELL AESRETLEGL QDNSRNIPDV
ADRASEETDR AIELRTRDRQ RKLVAKIDAA LRRIEEGEYG YCEVTGDPIS LKRLDARPIA
TMSLEAQEKH ERREKVHRDD
//
