MCPN_PSEAE
ID MCPN_PSEAE Reviewed; 531 AA.
AC Q9I055;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Methyl-accepting chemotaxis protein McpN {ECO:0000305};
GN Name=mcpN {ECO:0000303|PubMed:30782655};
GN OrderedLocusNames=PA2788 {ECO:0000312|EMBL:AAG06176.1};
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] {ECO:0007744|PDB:6GCV}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 44-179 IN COMPLEX WITH NITRATE,
RP FUNCTION, SUBUNIT, INDUCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF ARG-61.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=30782655; DOI=10.1128/mbio.02334-18;
RA Martin-Mora D., Ortega A., Matilla M.A., Martinez-Rodriguez S.,
RA Gavira J.A., Krell T.;
RT "The molecular mechanism of nitrate chemotaxis via direct ligand binding to
RT the PilJ domain of McpN.";
RL MBio 10:e02334-e02334(2019).
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. McpN is a chemoreceptor that recognizes specifically
CC nitrate and mediates chemoattraction. Binds nitrate specifically and
CC shows no affinity for other ligands such as nitrite. McpN-mediated
CC taxis occurs only under nitrate starvation conditions.
CC {ECO:0000269|PubMed:30782655}.
CC -!- SUBUNIT: Ligand free ligand-binding domain (LBD) is present in a
CC monomer-dimer equilibrium. Nitrate binding to the periplasmic LBD
CC stabilizes the homodimer. {ECO:0000269|PubMed:30782655}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:30782655}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is repressed in the presence of nitrate.
CC {ECO:0000269|PubMed:30782655}.
CC -!- DOMAIN: A single nitrate molecule is bound to a site on the dimer
CC symmetry axis. {ECO:0000269|PubMed:30782655}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not show nitrate chemotaxis.
CC {ECO:0000269|PubMed:30782655}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06176.1; -; Genomic_DNA.
DR PIR; D83297; D83297.
DR RefSeq; NP_251478.1; NC_002516.2.
DR RefSeq; WP_003114783.1; NZ_QZGE01000011.1.
DR PDB; 6GCV; X-ray; 1.30 A; A/B/C=44-179.
DR PDBsum; 6GCV; -.
DR AlphaFoldDB; Q9I055; -.
DR SMR; Q9I055; -.
DR STRING; 287.DR97_5159; -.
DR PaxDb; Q9I055; -.
DR PRIDE; Q9I055; -.
DR EnsemblBacteria; AAG06176; AAG06176; PA2788.
DR GeneID; 882783; -.
DR KEGG; pae:PA2788; -.
DR PATRIC; fig|208964.12.peg.2927; -.
DR PseudoCAP; PA2788; -.
DR HOGENOM; CLU_000445_107_27_6; -.
DR InParanoid; Q9I055; -.
DR OMA; LGMYWLM; -.
DR PhylomeDB; Q9I055; -.
DR BioCyc; PAER208964:G1FZ6-2836-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029095; NarX-like_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13675; PilJ; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chemotaxis; Membrane;
KW Methylation; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..531
FT /note="Methyl-accepting chemotaxis protein McpN"
FT /id="PRO_0000454719"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..174
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 201..254
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 259..495
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 52..140
FT /note="PilJ-type"
FT /evidence="ECO:0000305|PubMed:30782655"
FT MOTIF 54..65
FT /note="N-box"
FT /evidence="ECO:0000305|PubMed:30782655"
FT BINDING 61
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:30782655,
FT ECO:0007744|PDB:6GCV"
FT MUTAGEN 61
FT /note="R->A: Unable to recognize nitrate."
FT /evidence="ECO:0000269|PubMed:30782655"
FT HELIX 51..75
FT /evidence="ECO:0007829|PDB:6GCV"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:6GCV"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:6GCV"
FT HELIX 113..136
FT /evidence="ECO:0007829|PDB:6GCV"
FT HELIX 145..170
FT /evidence="ECO:0007829|PDB:6GCV"
SQ SEQUENCE 531 AA; 56389 MW; 5E71421A51AD5E63 CRC64;
MNESVARVFD RILRGLGLKT LNAQFLLSYA LMFGLAACAS VALYLSMSIS PETINVAGAQ
RMLSQKMARE ALQLRLGAGD PKALAATIAQ YERSAADLDA GNAERNVSRM GAPEIAAQRQ
KVAQIWGRYR AMLDQVAQPA SQVDLRGFSQ YSTELLGELN NLVSLMSARA DSVQHTQMWI
AFGCLLAILV LVVLGRQFGL APLMRQLRGL EVALTEVGAA NFTHALAAGH ADNEIGRIVA
GYERMRQDVS GLLANVKRSA AETDKDVAEA LEQALGAGDQ VARQHQDLDQ VATAMNEMSA
TVAEVARHAN HAAHSTRDAA ALAHEGRRLV EHASSQTGAL AEELEQTALA LNTLHQHAGS
VGQVLTVISS IAEQTNLLAL NAAIEAARAG EAGRGFAVVA DEVRSLANRT QQSTQEIQGL
IEQLQDGAND AVAAMRGSAS HAQSNLVEAD SAAQALGRIV ATVEELDGLN QQIATAAEEQ
SQVAQDIDRN ITNVSGLSEQ AHEGTAAVLS ANQRVKEHMA GLRVVLGRFR T
