DOSP_ECOLI
ID DOSP_ECOLI Reviewed; 799 AA.
AC P76129; P76872; P77708;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Oxygen sensor protein DosP;
DE EC=3.1.4.52;
DE AltName: Full=Direct oxygen-sensing phosphodiesterase;
DE Short=Direct oxygen sensor protein;
DE AltName: Full=Ec DOS;
DE AltName: Full=Heme-regulated cyclic di-GMP phosphodiesterase;
GN Name=dosP; Synonyms=dos, pdeO {ECO:0000303|PubMed:26148715}, yddU;
GN OrderedLocusNames=b1489, JW1484;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND HEME-BINDING.
RX PubMed=10704219; DOI=10.1021/bi991911s;
RA Delgado-Nixon V.M., Gonzalez G., Gilles-Gonzalez M.-A.;
RT "Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen
RT sensor.";
RL Biochemistry 39:2685-2691(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP MUTAGENESIS OF MET-87 AND ARG-89.
RX PubMed=12081490; DOI=10.1021/bi025845x;
RA Gonzalez G., Dioum E.M., Bertolucci C.M., Tomita T., Ikeda-Saito M.,
RA Cheesman M.R., Watmough N.J., Gilles-Gonzalez M.-A.;
RT "Nature of the displaceable heme-axial residue in the EcDos protein, a
RT heme-based sensor from Escherichia coli.";
RL Biochemistry 41:8414-8421(2002).
RN [6]
RP CHARACTERIZATION, HOMOTETRAMER SUBUNIT, AND MUTAGENESIS OF HIS-69 AND
RP HIS-75.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11970957; DOI=10.1074/jbc.m202738200;
RA Sasakura Y., Hirata S., Sugiyama S., Suzuki S., Taguchi S., Watanabe M.,
RA Matsui T., Sagami I., Shimizu T.;
RT "Characterization of a direct oxygen sensor heme protein from Escherichia
RT coli. Effects of the heme redox states and mutations at the heme-binding
RT site on catalysis and structure.";
RL J. Biol. Chem. 277:23821-23827(2002).
RN [7]
RP RESONANCE RAMAN SPECTROSCOPY, AND MUTAGENESIS OF MET-87.
RX PubMed=12080073; DOI=10.1074/jbc.m204559200;
RA Sato A., Sasakura Y., Sugiyama S., Sagami I., Shimizu T., Mizutani Y.,
RA Kitagawa T.;
RT "Stationary and time-resolved resonance Raman spectra of His77 and Met95
RT mutants of the isolated heme domain of a direct oxygen sensor from
RT Escherichia coli.";
RL J. Biol. Chem. 277:32650-32658(2002).
RN [8]
RP ABSORPTION SPECTROSCOPY.
RX PubMed=12767236; DOI=10.1021/bi027359f;
RA Liebl U., Bouzhir-Sima L., Kiger L., Marden M.C., Lambry J.-C.,
RA Negrerie M., Vos M.H.;
RT "Ligand binding dynamics to the heme domain of the oxygen sensor Dos from
RT Escherichia coli.";
RL Biochemistry 42:6527-6535(2003).
RN [9]
RP MUTAGENESIS OF HIS-69; HIS-582 AND HIS-586.
RX PubMed=14551206; DOI=10.1074/jbc.m304408200;
RA Yoshimura T., Sagami I., Sasakura Y., Shimizu T.;
RT "Relationships between heme incorporation, tetramer formation, and
RT catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a
RT study of deletion and site-directed mutants.";
RL J. Biol. Chem. 278:53105-53111(2003).
RN [10]
RP CHARACTERIZATION OF THE EAL DOMAIN AS A CYCLIC DINUCLEOTIDE DI-GMP
RP PHOSPHODIESTERASE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15995192; DOI=10.1128/jb.187.14.4774-4781.2005;
RA Schmidt A.J., Ryjenkov D.A., Gomelsky M.;
RT "The ubiquitous protein domain EAL is a cyclic diguanylate-specific
RT phosphodiesterase: enzymatically active and inactive EAL domains.";
RL J. Bacteriol. 187:4774-4781(2005).
RN [11]
RP CHARACTERIZATION OF CYCLIC DI-GMP ACTIVITY OF THE FULL-LENGTH PROTEIN.
RX DOI=10.1246/cl.2006.970;
RA Takahashi H., Shimizu T.;
RT "Phosphodiesterase activity of Ec DOS, a heme-regulated enzyme from
RT Escherichia coli, toward 3',5'-cyclic diguanylic acid is obviously enhanced
RT by O2 and CO binding.";
RL Chem. Lett. 35:970-971(2006).
RN [12]
RP MUTAGENESIS OF LEU-91 AND LEU-107.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=16519686; DOI=10.1111/j.1742-4658.2006.05145.x;
RA Yokota N., Araki Y., Kurokawa H., Ito O., Igarashi J., Shimizu T.;
RT "Critical roles of Leu99 and Leu115 at the heme distal side in auto-
RT oxidation and the redox potential of a heme-regulated phosphodiesterase
RT from Escherichia coli.";
RL FEBS J. 273:1210-1223(2006).
RN [13]
RP OPERON STRUCTURE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16418169; DOI=10.1074/jbc.m510701200;
RA Mendez-Ortiz M.M., Hyodo M., Hayakawa Y., Membrillo-Hernandez J.;
RT "Genome-wide transcriptional profile of Escherichia coli in response to
RT high levels of the second messenger 3',5'-cyclic diguanylic acid.";
RL J. Biol. Chem. 281:8090-8099(2006).
RN [14]
RP ROLE OF ARG-89 IN O(2) STABILIZATION, AND MUTAGENESIS OF MET-87 AND ARG-89.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=17535805; DOI=10.1074/jbc.m701920200;
RA Tanaka A., Takahashi H., Shimizu T.;
RT "Critical role of the heme axial ligand, Met95, in locking catalysis of the
RT phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP.";
RL J. Biol. Chem. 282:21301-21307(2007).
RN [15]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH DOSC, AND OPERON
RP STRUCTURE.
RX PubMed=19764732; DOI=10.1021/bi901409g;
RA Tuckerman J.R., Gonzalez G., Sousa E.H., Wan X., Saito J.A., Alam M.,
RA Gilles-Gonzalez M.A.;
RT "An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-
RT di-GMP control.";
RL Biochemistry 48:9764-9774(2009).
RN [16]
RP HOMODIMER SUBUNIT.
RX PubMed=19864414; DOI=10.1074/jbc.m109.066811;
RA Lechauve C., Bouzhir-Sima L., Yamashita T., Marden M.C., Vos M.H.,
RA Liebl U., Kiger L.;
RT "Heme ligand binding properties and intradimer interactions in the full-
RT length sensor protein dos from Escherichia coli and its isolated heme
RT domain.";
RL J. Biol. Chem. 284:36146-36159(2009).
RN [17]
RP INDUCTION, AND RPOS-DEPENDENCE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19332833; DOI=10.1099/mic.0.024257-0;
RA Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N.,
RA Hengge R.;
RT "Gene expression patterns and differential input into curli fimbriae
RT regulation of all GGDEF/EAL domain proteins in Escherichia coli.";
RL Microbiology 155:1318-1331(2009).
RN [18]
RP FUNCTION IN REGULATION OF CSGBAC EXPRESSION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20553324; DOI=10.1111/j.1574-695x.2010.00702.x;
RA Tagliabue L., Maciag A., Antoniani D., Landini P.;
RT "The yddV-dos operon controls biofilm formation through the regulation of
RT genes encoding curli fibers' subunits in aerobically growing Escherichia
RT coli.";
RL FEMS Immunol. Med. Microbiol. 59:477-484(2010).
RN [19]
RP NOMENCLATURE.
RX PubMed=26148715; DOI=10.1128/jb.00424-15;
RA Hengge R., Galperin M.Y., Ghigo J.M., Gomelsky M., Green J., Hughes K.T.,
RA Jenal U., Landini P.;
RT "Systematic nomenclature for GGDEF and EAL domain-containing cyclic di-GMP
RT turnover proteins of Escherichia coli.";
RL J. Bacteriol. 198:7-11(2015).
RN [20]
RP CRYSTALLIZATION OF 1-139.
RC STRAIN=K12;
RX PubMed=12198316; DOI=10.1107/s0907444902011794;
RA Park H., Suquet C., Savenkova M.I., Satterlee J.D., Kang C.;
RT "Cloning, purification, crystallization and preliminary X-ray analysis of
RT DOS heme domain, a new heme oxygen sensor in Escherichia coli.";
RL Acta Crystallogr. D 58:1504-1506(2002).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-136 IN COMPLEX WITH AND WITHOUT
RP O(2).
RC STRAIN=K12;
RX PubMed=15005609; DOI=10.1021/bi035980p;
RA Park H., Suquet C., Satterlee J.D., Kang C.;
RT "Insights into signal transduction involving PAS domain oxygen-sensing heme
RT proteins from the X-ray crystal structure of Escherichia coli Dos heme
RT domain (Ec DosH).";
RL Biochemistry 43:2738-2746(2004).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 1-139 IN AN ACTIVE FE(2+)-BOUND
RP FORM, AND INACTIVE FE(3+)-BOUND FORM.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=14982921; DOI=10.1074/jbc.m314199200;
RA Kurokawa H., Lee D.-S., Watanabe M., Sagami I., Mikami B., Raman C.S.,
RA Shimizu T.;
RT "A redox-controlled molecular switch revealed by the crystal structure of a
RT bacterial heme PAS sensor.";
RL J. Biol. Chem. 279:20186-20193(2004).
CC -!- FUNCTION: Heme-based oxygen sensor protein displaying phosphodiesterase
CC (PDE) activity toward c-di-GMP in response to oxygen availability.
CC Involved in the modulation of intracellular c-di-GMP levels, in
CC association with DosC which catalyzes the biosynthesis of c-di-GMP
CC (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger
CC which controls cell surface-associated traits in bacteria. Has very
CC poor PDE activity on cAMP (PubMed:15995192) but is not active with
CC cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate
CC (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates
CC biofilm formation through the repression of transcription of the csgBAC
CC operon, which encodes curli structural subunits.
CC {ECO:0000269|PubMed:11970957, ECO:0000269|PubMed:15995192,
CC ECO:0000269|PubMed:20553324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclic di-3',5'-guanylate + H2O = 5'-
CC phosphoguanylyl(3'->5')guanosine + H(+); Xref=Rhea:RHEA:24902,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58754,
CC ChEBI:CHEBI:58805; EC=3.1.4.52;
CC Evidence={ECO:0000269|PubMed:19764732};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Has c-di-GMP PDE activity in both Fe(2+) and
CC Fe(3+)-bound forms; this activity is increased 6-7 fold by binding of
CC O(2) and CO (PubMed:15995192) and NO (PubMed:17535805). Has cAMP PDE
CC activity only when the heme is in the Fe(2+) form. cAMP PDE activity is
CC inhibited by oxidation of the heme iron and by binding of external
CC ligands such as CO and NO. Also strongly inhibited by etazolate
CC hydrochloride, a selective cAMP PDE inhibitor. PDE activity is
CC inhibited in the absence of oxygen. {ECO:0000269|PubMed:15995192,
CC ECO:0000269|PubMed:17535805, ECO:0000269|PubMed:19764732}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for c-di-GMP;
CC Note=For the EAL domain, residues 532-799.
CC {ECO:0000269|PubMed:15995192};
CC -!- SUBUNIT: Homodimer (PubMed:19864414); has been previously suggested to
CC be a homotetramer based on size exclusion chromatography
CC (PubMed:11970957). Forms a complex with DosC.
CC {ECO:0000269|PubMed:11970957, ECO:0000269|PubMed:15005609,
CC ECO:0000269|PubMed:19864414}.
CC -!- INDUCTION: Expressed in the late exponential growth phase and at higher
CC levels in the stationary phase. A member of the dosCP operon.
CC Expression is RpoS dependent and is higher at 28 degrees Celsius than
CC at 37 degrees Celsius. {ECO:0000269|PubMed:19332833,
CC ECO:0000269|PubMed:20553324}.
CC -!- DOMAIN: The EAL domain (residues 532 to 799) is a cyclic dinucleotide
CC di-GMP (c-di-GMP) PDE hydrolyzing c-di-GMP to 5'pGpG; it has no
CC activity on cAMP. {ECO:0000269|PubMed:15995192}.
CC -!- DOMAIN: Binding of an external ligand to the heme located in the N-
CC terminal sensory domain displaces the distal heme ligand from Met-87 to
CC the ligand and triggers a conformational change that regulates the
CC activity of the C-terminal catalytic domain.
CC -!- DOMAIN: The heme-PAS domain (residues 1-139) forms homodimers.
CC -!- PTM: The heme distal ligand is coordinated by Met-87 in the active
CC Fe(2+) (ferrous) form, by O(2) in the O(2)-bound form and by H(2)O in
CC the inactive Fe(3+) (ferric) form.
CC -!- MISCELLANEOUS: Binds O(2) with a dissociation constant of about 74 uM.
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DR EMBL; U00096; AAC74562.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15154.1; -; Genomic_DNA.
DR PIR; D64902; D64902.
DR RefSeq; NP_416006.4; NC_000913.3.
DR RefSeq; WP_001360132.1; NZ_LN832404.1.
DR PDB; 1S66; X-ray; 1.80 A; L/U=8-126.
DR PDB; 1S67; X-ray; 1.50 A; L/U=8-126.
DR PDB; 1V9Y; X-ray; 1.32 A; A/B=1-139.
DR PDB; 1V9Z; X-ray; 1.90 A; A/B=1-139.
DR PDB; 1VB6; X-ray; 1.56 A; A/B=1-139.
DR PDB; 4HU3; X-ray; 3.30 A; A=529-799.
DR PDB; 4HU4; X-ray; 2.40 A; A/B=529-799.
DR PDBsum; 1S66; -.
DR PDBsum; 1S67; -.
DR PDBsum; 1V9Y; -.
DR PDBsum; 1V9Z; -.
DR PDBsum; 1VB6; -.
DR PDBsum; 4HU3; -.
DR PDBsum; 4HU4; -.
DR AlphaFoldDB; P76129; -.
DR SMR; P76129; -.
DR BioGRID; 4259419; 16.
DR BioGRID; 850182; 1.
DR ComplexPortal; CPX-3982; dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex.
DR IntAct; P76129; 3.
DR STRING; 511145.b1489; -.
DR PaxDb; P76129; -.
DR PRIDE; P76129; -.
DR EnsemblBacteria; AAC74562; AAC74562; b1489.
DR EnsemblBacteria; BAA15154; BAA15154; BAA15154.
DR GeneID; 945815; -.
DR KEGG; ecj:JW1484; -.
DR KEGG; eco:b1489; -.
DR PATRIC; fig|1411691.4.peg.778; -.
DR EchoBASE; EB3553; -.
DR eggNOG; COG2199; Bacteria.
DR eggNOG; COG2200; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR HOGENOM; CLU_000445_70_20_6; -.
DR InParanoid; P76129; -.
DR OMA; WHDPVLG; -.
DR PhylomeDB; P76129; -.
DR BioCyc; EcoCyc:G6783-MON; -.
DR BioCyc; MetaCyc:G6783-MON; -.
DR SABIO-RK; P76129; -.
DR EvolutionaryTrace; P76129; -.
DR PRO; PR:P76129; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0071111; F:cyclic-guanylate-specific phosphodiesterase activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IMP:EcoCyc.
DR GO; GO:0019826; F:oxygen sensor activity; IDA:CACAO.
DR GO; GO:0070482; P:response to oxygen levels; IDA:ComplexPortal.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.20.20.450; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR012226; Diguanyl_cyclase/Pdiesterase.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PIRSF; PIRSF005925; Dos; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF141868; SSF141868; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; c-di-GMP; Heme; Hydrolase; Iron; Magnesium; Metal-binding;
KW Reference proteome; Repeat; Sensory transduction; Transcription;
KW Transcription regulation.
FT CHAIN 1..799
FT /note="Oxygen sensor protein DosP"
FT /id="PRO_0000079982"
FT DOMAIN 10..81
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 134..207
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 208..260
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 402..532
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT DOMAIN 541..795
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT BINDING 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT MUTAGEN 69
FT /note="H->A,G: Loss of heme binding."
FT /evidence="ECO:0000269|PubMed:11970957,
FT ECO:0000269|PubMed:14551206"
FT MUTAGEN 75
FT /note="H->A,G: No loss of heme binding."
FT /evidence="ECO:0000269|PubMed:11970957"
FT MUTAGEN 87
FT /note="M->A,I: Ferrous heme iron changes from an
FT exclusively hexacoordinate low-spin form to an exclusively
FT pentacoordinate high-spin form. Ferric heme iron remains
FT hexacoordinate but becomes a mixture of high and low spin.
FT Increases c-di-GMP PDE activity 7-fold in absence of O(2),
FT CO or NO, no additional increase upon addition of gases (M-
FT A only)."
FT /evidence="ECO:0000269|PubMed:12080073,
FT ECO:0000269|PubMed:12081490, ECO:0000269|PubMed:17535805"
FT MUTAGEN 87
FT /note="M->H: No change in heme coordination; increases c-
FT di-GMP PDE activity 2-fold in absence of O(2), CO or NO,
FT and 2-fold more upon addition of gases."
FT /evidence="ECO:0000269|PubMed:12080073,
FT ECO:0000269|PubMed:12081490, ECO:0000269|PubMed:17535805"
FT MUTAGEN 89
FT /note="R->A,E,I: The Fe(2+)-O(2) form loses c-di-GMP PDE
FT activity, due to reduced O(2) affinity and/or increased
FT auto-oxidation. NO and CO forms are less affected."
FT /evidence="ECO:0000269|PubMed:12081490,
FT ECO:0000269|PubMed:17535805"
FT MUTAGEN 91
FT /note="L->F: Alters O(2) binding, increases auto-
FT oxidation."
FT /evidence="ECO:0000269|PubMed:16519686"
FT MUTAGEN 91
FT /note="L->T: Increases auto-oxidation."
FT /evidence="ECO:0000269|PubMed:16519686"
FT MUTAGEN 107
FT /note="L->F: Significantly reduces heme-binding affinity;
FT increases auto-oxidation."
FT /evidence="ECO:0000269|PubMed:16519686"
FT MUTAGEN 107
FT /note="L->T: Increases auto-oxidation."
FT /evidence="ECO:0000269|PubMed:16519686"
FT MUTAGEN 582
FT /note="H->A: Loss of cAMP PDE activity."
FT /evidence="ECO:0000269|PubMed:14551206"
FT MUTAGEN 586
FT /note="H->A: Loss of cAMP PDE activity."
FT /evidence="ECO:0000269|PubMed:14551206"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:1V9Y"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:1V9Y"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1V9Y"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:1V9Y"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1V9Y"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1V9Y"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1V9Y"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1V9Y"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1V9Y"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:1V9Y"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1V9Y"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1S67"
FT STRAND 100..112
FT /evidence="ECO:0007829|PDB:1V9Y"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:1V9Y"
FT HELIX 544..549
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 557..569
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 572..583
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 607..623
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 637..640
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 648..656
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 703..707
FT /evidence="ECO:0007829|PDB:4HU3"
FT TURN 708..711
FT /evidence="ECO:0007829|PDB:4HU3"
FT STRAND 715..719
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 721..729
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 731..746
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 750..754
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 759..767
FT /evidence="ECO:0007829|PDB:4HU4"
FT STRAND 772..775
FT /evidence="ECO:0007829|PDB:4HU4"
FT TURN 776..778
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:4HU4"
FT HELIX 787..793
FT /evidence="ECO:0007829|PDB:4HU4"
SQ SEQUENCE 799 AA; 90260 MW; 4CE770D2A6B39D5F CRC64;
MKLTDADNAA DGIFFPALEQ NMMGAVLINE NDEVMFFNPA AEKLWGYKRE EVIGNNIDML
IPRDLRPAHP EYIRHNREGG KARVEGMSRE LQLEKKDGSK IWTRFALSKV SAEGKVYYLA
LVRDASVEMA QKEQTRQLII AVDHLDRPVI VLDPERHIVQ CNRAFTEMFG YCISEASGMQ
PDTLLNIPEF PADNRIRLQQ LLWKTARDQD EFLLLTRTGE KIWIKASISP VYDVLAHLQN
LVMTFSDITE ERQIRQLEGN ILAAMCSSPP FHEMGEIICR NIESVLNESH VSLFALRNGM
PIHWASSSHG AEIQNAQSWS ATIRQRDGAP AGILQIKTSS GAETSAFIER VADISQHMAA
LALEQEKSRQ HIEQLIQFDP MTGLPNRNNL HNYLDDLVDK AVSPVVYLIG VDHIQDVIDS
LGYAWADQAL LEVVNRFREK LKPDQYLCRI EGTQFVLVSL ENDVSNITQI ADELRNVVSK
PIMIDDKPFP LTLSIGISYD LGKNRDYLLS TAHNAMDYIR KNGGNGWQFF SPAMNEMVKE
RLVLGAALKE AISNNQLKLV YQPQIFAETG ELYGIEALAR WHDPLHGHVP PSRFIPLAEE
IGEIENIGRW VIAEACRQLA EWRSQNIHIP ALSVNLSALH FRSNQLPNQV SDAMHAWGID
GHQLTVEITE SMMMEHDTEI FKRIQILRDM GVGLSVDDFG TGFSGLSRLV SLPVTEIKID
KSFVDRCLTE KRILALLEAI TSIGQSLNLT VVAEGVETKE QFEMLRKIHC RVIQGYFFSR
PLPAEEIPGW MSSVLPLKI
