FLEN_PSEAE
ID FLEN_PSEAE Reviewed; 280 AA.
AC G3XD64;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Antiactivator FleN {ECO:0000303|PubMed:28065505};
GN Name=fleN {ECO:0000303|PubMed:28065505}; OrderedLocusNames=PA1454;
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 [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).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10629180; DOI=10.1128/jb.182.2.357-364.2000;
RA Dasgupta N., Arora S.K., Ramphal R.;
RT "fleN, a gene that regulates flagellar number in Pseudomonas aeruginosa.";
RL J. Bacteriol. 182:357-364(2000).
RN [3]
RP FUNCTION, AND INTERACTION WITH FLEQ.
RX PubMed=22581773; DOI=10.1093/nar/gks384;
RA Baraquet C., Murakami K., Parsek M.R., Harwood C.S.;
RT "The FleQ protein from Pseudomonas aeruginosa functions as both a repressor
RT and an activator to control gene expression from the pel operon promoter in
RT response to c-di-GMP.";
RL Nucleic Acids Res. 40:7207-7218(2012).
RN [4] {ECO:0007744|PDB:5J1J, ECO:0007744|PDB:5JVF}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT,
RP ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=28065505; DOI=10.1016/j.str.2016.11.022;
RA Chanchal X., Banerjee P., Jain D.;
RT "ATP-Induced Structural Remodeling in the Antiactivator FleN Enables
RT Formation of the Functional Dimeric Form.";
RL Structure 25:243-252(2017).
CC -!- FUNCTION: ATPase that plays an important role in maintaining flagellar
CC number in Pseudomonas aeruginosa (PubMed:10629180, PubMed:28065505).
CC Exhibits anti-activator activity against FleQ, the global
CC transcriptional regulator of flagellar genes (PubMed:22581773,
CC PubMed:28065505). {ECO:0000269|PubMed:10629180,
CC ECO:0000269|PubMed:22581773, ECO:0000269|PubMed:28065505}.
CC -!- ACTIVITY REGULATION: ATP-binding allows dimerization and subsequent
CC antagonistic effect against FleQ. {ECO:0000269|PubMed:28065505}.
CC -!- SUBUNIT: Forms homodimers (PubMed:28065505). Interacts with FleQ
CC (PubMed:22581773). {ECO:0000269|PubMed:22581773,
CC ECO:0000269|PubMed:28065505}.
CC -!- DISRUPTION PHENOTYPE: Deletion results in up-regulation of flagellar
CC genes that code for structural and regulatory proteins, leading to the
CC multi-flagellated phenotype, which shows motility defect.
CC {ECO:0000269|PubMed:10629180}.
CC -!- SIMILARITY: Belongs to the ParA family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04843.1; -; Genomic_DNA.
DR PIR; B83463; B83463.
DR RefSeq; NP_250145.1; NC_002516.2.
DR RefSeq; WP_003083064.1; NZ_QZGE01000005.1.
DR PDB; 5J1J; X-ray; 1.55 A; A/B=1-280.
DR PDB; 5JVF; X-ray; 1.66 A; A=1-280.
DR PDB; 7EJW; X-ray; 1.98 A; A/B=1-280.
DR PDBsum; 5J1J; -.
DR PDBsum; 5JVF; -.
DR PDBsum; 7EJW; -.
DR AlphaFoldDB; G3XD64; -.
DR SMR; G3XD64; -.
DR STRING; 287.DR97_569; -.
DR PaxDb; G3XD64; -.
DR PRIDE; G3XD64; -.
DR EnsemblBacteria; AAG04843; AAG04843; PA1454.
DR GeneID; 881866; -.
DR KEGG; pae:PA1454; -.
DR PATRIC; fig|208964.12.peg.1505; -.
DR PseudoCAP; PA1454; -.
DR HOGENOM; CLU_037612_0_0_6; -.
DR InParanoid; G3XD64; -.
DR OMA; FKVAKNN; -.
DR PhylomeDB; G3XD64; -.
DR BioCyc; PAER208964:G1FZ6-1480-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:PseudoCAP.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051782; P:negative regulation of cell division; IBA:GO_Central.
DR CDD; cd02038; FlhG-like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR033875; FlhG.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR Pfam; PF10609; ParA; 1.
DR PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..280
FT /note="Antiactivator FleN"
FT /id="PRO_0000448539"
FT BINDING 19..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:28065505,
FT ECO:0007744|PDB:5J1J"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:28065505,
FT ECO:0007744|PDB:5J1J"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:28065505,
FT ECO:0007744|PDB:5J1J"
FT BINDING 215..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:28065505,
FT ECO:0007744|PDB:5J1J"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:28065505,
FT ECO:0007744|PDB:5J1J"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5J1J"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:5J1J"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:5J1J"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:5JVF"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:5J1J"
SQ SEQUENCE 280 AA; 30037 MW; AE42DAEDF0BA1B0C CRC64;
MKQMGSMHPV QVIAVTGGKG GVGKTNVSVN LALALADLGR RVMLLDADLG LANVDVLLGL
TPKRTLADVI EGRCELRDVL LLGPGGVRIV PAASGTQSMV HLSPMQHAGL IQAFSDISDN
LDVLVVDTAA GIGDSVVSFV RAAQEVLLVV CDEPTSITDA YALIKLLNRD HGMTRFRVLA
NMAHSPQEGR NLFAKLTKVT DRFLDVALQY VGVIPYDESV RKAVQKQRAV YEAFPRSKAS
LAFKAVAQKV DSWPLPANPR GHLEFFVERL VQHPATGSAV
