ID   SFNR_PSEPU              Reviewed;         366 AA.
AC   Q845S7;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Sigma54-dependent transcriptional activator SfnR {ECO:0000303|PubMed:12686641};
GN   Name=sfnR {ECO:0000312|EMBL:BAC66053.1};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303 {ECO:0000312|EMBL:BAC66053.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAC66053.1};
RX   PubMed=12835925; DOI=10.1007/s00253-003-1233-7;
RA   Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H.,
RA   Omori T.;
RT   "Characterization and identification of genes essential for dimethyl
RT   sulfide utilization in Pseudomonas putida strain DS1.";
RL   Appl. Microbiol. Biotechnol. 62:83-91(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAC66053.1};
RX   PubMed=12686641; DOI=10.1099/mic.0.26031-0;
RA   Endoh T., Habe H., Yoshida T., Nojiri H., Omori T.;
RT   "A CysB-regulated and sigma54-dependent regulator, SfnR, is essential for
RT   dimethyl sulfone metabolism of Pseudomonas putida strain DS1.";
RL   Microbiology 149:991-1000(2003).
RN   [3]
RP   FUNCTION.
RC   STRAIN=DS1;
RX   PubMed=15661012; DOI=10.1111/j.1365-2958.2004.04431.x;
RA   Endoh T., Habe H., Nojiri H., Yamane H., Omori T.;
RT   "The sigma54-dependent transcriptional activator SfnR regulates the
RT   expression of the Pseudomonas putida sfnFG operon responsible for dimethyl
RT   sulphone utilization.";
RL   Mol. Microbiol. 55:897-911(2005).
CC   -!- FUNCTION: Involved in the dimethyl sulfide degradation pathway
CC       (PubMed:12686641). Activates the expression of sfnG and sfnF.
CC       {ECO:0000269|PubMed:12686641, ECO:0000269|PubMed:15661012}.
CC   -!- INDUCTION: Under sulfate limitation conditions, it is transcriptionally
CC       activated by the LysR-type transcriptional regulator, CysB.
CC       {ECO:0000269|PubMed:12686641}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are still able to convert
CC       dimethyl sulfide (DMS) to dimethyl sulfone (DMSO2) under sulfate
CC       limitation, suggesting that the conversion of dimethyl sulfone (DMSO2)
CC       to methanesulfonate (MSA) is interrupted in this mutant.
CC       {ECO:0000269|PubMed:12686641}.
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; AB091764; BAC66053.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q845S7; -.
DR   SMR; Q845S7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   2: Evidence at transcript level;
KW   Activator; ATP-binding; DNA-binding; Nucleotide-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..366
FT                   /note="Sigma54-dependent transcriptional activator SfnR"
FT                   /id="PRO_0000443543"
FT   DOMAIN          21..250
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         112..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
SQ   SEQUENCE   366 AA;  40778 MW;  0DE2B34FCF847CBE CRC64;
     MQLLTLPPSP TLATSIRATA QVFEDPRSQA LLAHLQQVAP SEASVLIIGE TGTGKELVAR
     HIHNLSGRRN GPFVAVNCGA FSESLVEAEL FGHEKGAFTG ALAAKAGWFE EANGGTLFLD
     EIGDLPLPIQ VKLLRVLQER EVVRLGSRKS IPINVRVLAA TNVQLEKAIN AGHFREDLYY
     RLNVVTLQLH PLRDRPGDIL PLARHFIRSY SDRLGYGPVE LSAKAQAKLV EYSWPGNIRE
     LENVIHHSLL TCGDGTVQAQ DLRLSNLRIE RQEEEPAGNG VEDLLQRAFS RLYEEQSGDL
     YEKVENALLR SAYRFCHYNQ VHTAQLLGLS RNITRTRLIA IGELVVNKRR GQEQQVLDNR
     VVRLSI