MCPK_PSEAE
ID MCPK_PSEAE Reviewed; 647 AA.
AC Q9HUB1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Methyl-accepting chemotaxis protein McpK {ECO:0000305};
DE AltName: Full=Methyl-accepting chemotaxis protein K {ECO:0000303|PubMed:27965656};
GN Name=mcpK {ECO:0000303|PubMed:27965656};
GN OrderedLocusNames=PA5072 {ECO:0000312|EMBL:AAG08457.1};
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]
RP FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27965656; DOI=10.3389/fmicb.2016.01937;
RA Martin-Mora D., Ortega A., Reyes-Darias J.A., Garcia V., Lopez-Farfan D.,
RA Matilla M.A., Krell T.;
RT "Identification of a chemoreceptor in Pseudomonas aeruginosa that
RT specifically mediates chemotaxis toward alpha-ketoglutarate.";
RL Front. Microbiol. 7:1937-1937(2016).
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. McpK is a chemoreceptor that specifically binds and
CC mediates chemotaxis to alpha-ketoglutarate (alphaKG).
CC {ECO:0000269|PubMed:27965656}.
CC -!- SUBUNIT: Ligand free ligand-binding domain (LBD) is present in a
CC monomer-dimer equilibrium. AlphaKG binding stabilizes the homodimer.
CC {ECO:0000269|PubMed:27965656}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:27965656}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression of the gene is not regulated by the presence of
CC alphaKG. {ECO:0000269|PubMed:27965656}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in a drop in the
CC chemotactic response toward alphaKG to close to background levels, but
CC does not alter maize root colonization. {ECO:0000269|PubMed:27965656}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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; AE004091; AAG08457.1; -; Genomic_DNA.
DR PIR; C83012; C83012.
DR RefSeq; NP_253759.1; NC_002516.2.
DR RefSeq; WP_003115040.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUB1; -.
DR SMR; Q9HUB1; -.
DR STRING; 287.DR97_2427; -.
DR PaxDb; Q9HUB1; -.
DR EnsemblBacteria; AAG08457; AAG08457; PA5072.
DR GeneID; 881232; -.
DR KEGG; pae:PA5072; -.
DR PATRIC; fig|208964.12.peg.5317; -.
DR PseudoCAP; PA5072; -.
DR HOGENOM; CLU_000445_107_27_6; -.
DR InParanoid; Q9HUB1; -.
DR OMA; IDRSNWM; -.
DR PhylomeDB; Q9HUB1; -.
DR BioCyc; PAER208964:G1FZ6-5188-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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR032255; HBM.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF16591; HBM; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM01358; HBM; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS51753; HBM; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..647
FT /note="Methyl-accepting chemotaxis protein McpK"
FT /id="PRO_0000454718"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..291
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:27965656"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 45..287
FT /note="HBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01089"
FT DOMAIN 314..370
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 375..611
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ SEQUENCE 647 AA; 69701 MW; BC60C7377A256209 CRC64;
MYDWWVLQLA KLSVSRKLMV GFGVLLALLL LVVISSNRTL THQTALSEQL AEVASLMEQT
QQAEQGRLAF EAGSDPRQAE QVRQTLAGML QRLQALRDSE LDPAALAHQV EAIEAYRKAF
DDLAAADQQR SAARGVLVGT AQQALDSFAR LEELMDASLA QQAGDPQALQ RSRAVADLHQ
QLLMVRYQVR GYVFERSDKA EQAAFAAFDA LRQAATTLRG QLPGEADAAL EQAMGSLQGY
RGGIEQFRAG VIRTRQAQQA MQSSTQDMAR AGRTLTEAGR QLRESTASRD RASLWLIAAL
ALAFGCVAGW AINRQIVRPL DEALAQAEAI AAGDLGKRPQ NPLTLQRRDE LGQLQRVMQR
MGDSLRELVG RISDGVSQLA SSAEELSAVT EQTRAGVNSQ KVETDQVATA MHEMAATVQD
VARNAELASQ AARQADEEAR QGDAVVDQAV TRIERLASEM DVSSEAMARL KNESEQIGSV
LDVIKSVAEQ TNLLALNAAI EAARAGDAGR GFAVVADEVR GLAQRTQQST AEIEGLIQRL
QQGAGEAAER LENSRSLTAS TVELARRAGA ALDSITRTVS DIQNMNLQIA TAAEQQSTVA
EEINRSVLSV RDVAEQSAAA SEQTAASSGE LARLGTQLQA QVGRFRL
