NIRQ_PSEAE
ID NIRQ_PSEAE Reviewed; 260 AA.
AC Q51481;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Denitrification regulatory protein NirQ;
GN Name=nirQ; OrderedLocusNames=PA0520;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO1161;
RX PubMed=7765251; DOI=10.1271/bbb.58.1286;
RA Arai H., Igarashi Y., Kodama T.;
RT "Structure and ANR-dependent transcription of the nir genes for
RT denitrification from Pseudomonas aeruginosa.";
RL Biosci. Biotechnol. Biochem. 58:1286-1291(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Activator of nitrite and nitric oxide reductases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Under denitrifying conditions.
CC -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family. {ECO:0000305}.
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DR EMBL; D37883; BAA07123.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03909.1; -; Genomic_DNA.
DR PIR; JC2288; JC2288.
DR RefSeq; NP_249211.1; NC_002516.2.
DR RefSeq; WP_003113240.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; Q51481; -.
DR SMR; Q51481; -.
DR STRING; 287.DR97_3488; -.
DR PaxDb; Q51481; -.
DR PRIDE; Q51481; -.
DR EnsemblBacteria; AAG03909; AAG03909; PA0520.
DR GeneID; 882214; -.
DR KEGG; pae:PA0520; -.
DR PATRIC; fig|208964.12.peg.550; -.
DR PseudoCAP; PA0520; -.
DR HOGENOM; CLU_067562_0_0_6; -.
DR InParanoid; Q51481; -.
DR OMA; CALFEHA; -.
DR PhylomeDB; Q51481; -.
DR BioCyc; PAER208964:G1FZ6-525-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR013615; CbbQ_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF08406; CbbQ_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..260
FT /note="Denitrification regulatory protein NirQ"
FT /id="PRO_0000219569"
FT DNA_BIND 234..253
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 260 AA; 28904 MW; 3FD36F19BEBA38B5 CRC64;
MRDATPFYEA TGHEIEVFER AWRHGLPVLL KGPTGCGKTR FVQYMARRLE LPLYSVACHD
DLGAADLLGR HLIGADGTWW QDGPLTRAVR EGGICYLDEV VEARQDTTVA IHPLADDRRE
LYLERTGETL QAPPSFMLVV SYNPGYQNLL KGLKPSTRQR FVALRFDYPA AQQEARILVG
ESGCAETLAQ RLVQLGQALR RLEQHDLEEV ASTRLLIFAA RLIGDGMDPR EACRVALAEP
LSDDPATVAA LMDIVDLHVA