ID   ANR_PSEPH               Reviewed;         244 AA.
AC   O85222;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Transcriptional activator protein Anr {ECO:0000303|PubMed:9620970};
DE            Short=ANR {ECO:0000303|PubMed:9620970};
DE   AltName: Full=Anaerobic regulatory protein {ECO:0000312|EMBL:AAC38593.1};
GN   Name=anr {ECO:0000312|EMBL:AAC38593.1};
OS   Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1124983;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC38593.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX   PubMed=9620970; DOI=10.1128/jb.180.12.3187-3196.1998;
RA   Laville J., Blumer C., Von Schroetter C., Gaia V., Defago G., Keel C.,
RA   Haas D.;
RT   "Characterization of the hcnABC gene cluster encoding hydrogen cyanide
RT   synthase and anaerobic regulation by ANR in the strictly aerobic biocontrol
RT   agent Pseudomonas fluorescens CHA0.";
RL   J. Bacteriol. 180:3187-3196(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX   PubMed=10570200; DOI=10.1073/pnas.96.24.14073;
RA   Blumer C., Heeb S., Pessi G., Haas D.;
RT   "Global GacA-steered control of cyanide and exoprotease production in
RT   Pseudomonas fluorescens involves specific ribosome binding sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14073-14078(1999).
RN   [3]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX   PubMed=11021918; DOI=10.1099/00221287-146-10-2417;
RA   Blumer C., Haas D.;
RT   "Iron regulation of the hcnABC genes encoding hydrogen cyanide synthase
RT   depends on the anaerobic regulator ANR rather than on the global activator
RT   GacA in Pseudomonas fluorescens CHA0.";
RL   Microbiology 146:2417-2424(2000).
CC   -!- FUNCTION: Transcriptional activator of anaerobic gene expression.
CC       Regulates the expression of the components of the hydrogen cyanide
CC       synthase (HcnABC) in a positive manner (PubMed:10570200). May also act
CC       as an iron sensor. {ECO:0000269|PubMed:11021918,
CC       ECO:0000269|PubMed:9620970, ECO:0000305|PubMed:10570200}.
CC   -!- INDUCTION: Up-regulated by Fe(3+) levels in oxygen-limiting conditions.
CC       {ECO:0000269|PubMed:11021918, ECO:0000269|PubMed:9620970}.
CC   -!- DISRUPTION PHENOTYPE: Nearly complete loss of expression of hcnA
CC       (PubMed:10570200). {ECO:0000269|PubMed:10570200}.
CC   -!- MISCELLANEOUS: Possesses 4 cysteines which may bind a metal ion
CC       (possibly iron). {ECO:0000250|UniProtKB:P23926}.
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; AF053611; AAC38593.1; -; Genomic_DNA.
DR   RefSeq; WP_011060230.1; NZ_LS999205.1.
DR   AlphaFoldDB; O85222; -.
DR   SMR; O85222; -.
DR   GeneID; 57474937; -.
DR   PATRIC; fig|1124983.3.peg.1972; -.
DR   eggNOG; COG0664; Bacteria.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00092; HTH_CRP; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR012318; HTH_CRP.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR24567:SF75; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF13545; HTH_Crp_2; 1.
DR   PRINTS; PR00034; HTHCRP.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00419; HTH_CRP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS00042; HTH_CRP_1; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Iron; Transcription; Transcription regulation.
FT   CHAIN           1..244
FT                   /note="Transcriptional activator protein Anr"
FT                   /id="PRO_0000419765"
FT   DOMAIN          159..232
FT                   /note="HTH crp-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   DNA_BIND        192..211
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACJ8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00387"
FT   BINDING         21..149
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /evidence="ECO:0000250|UniProtKB:P23926,
FT                   ECO:0000255|PROSITE-ProRule:PRU00060"
SQ   SEQUENCE   244 AA;  27155 MW;  867AC251594A051F CRC64;
     MSEPVKLRAH NQAHCKDCSL APLCLPLSLN LEDMDALDEI VKRGRPLKKG EFLFRQGDGF
     DSVYAVRSGA LKTFSLSDSG EEQITGFHLP SELVGLSGMD TESHPVSAQA LETTSVCEIP
     FERLDELALQ LPQLRRQLMR VMSREIRDDQ QMMLLLSKKT ADERIATFLV NLSARFRARG
     FSANQFRLSM SRNEIGNYLG LAVETVSRVF TRFQQNELIA AEGKEVHILD PIQLCALAGG
     SVEG
//