GenomeNet

Database: UniProt
Entry: A0A1I3BHM1_9RHOB
LinkDB: A0A1I3BHM1_9RHOB
Original site: A0A1I3BHM1_9RHOB 
ID   A0A1I3BHM1_9RHOB        Unreviewed;       140 AA.
AC   A0A1I3BHM1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN04488021_1229 {ECO:0000313|EMBL:SFH61773.1};
OS   Paracoccus aminovorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH61773.1, ECO:0000313|Proteomes:UP000183635};
RN   [1] {ECO:0000313|EMBL:SFH61773.1, ECO:0000313|Proteomes:UP000183635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH61773.1,
RC   ECO:0000313|Proteomes:UP000183635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOPU01000022; SFH61773.1; -; Genomic_DNA.
DR   RefSeq; WP_074968602.1; NZ_LN832559.1.
DR   AlphaFoldDB; A0A1I3BHM1; -.
DR   STRING; 34004.SAMN04488021_1229; -.
DR   OrthoDB; 9803742at2; -.
DR   Proteomes; UP000183635; 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:UP000183635};
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"
FT   REGION          48..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   140 AA;  16625 MW;  A4615EBD406F9A08 CRC64;
     MKAQTFLPED YRPAEDEPFM NERQLEYFRR KLIAWKQELL DQSAETLEGL QDSARNVPDL
     ADRASEETDR SLELRTRDRQ RKLVSKIDSA LRRIETGEYG YCEMTGEPIS LKRLDARPIA
     TMTLEAQERH ERRERVHRDD
//
DBGET integrated database retrieval system