PCTC_PSEAE
ID PCTC_PSEAE Reviewed; 632 AA.
AC Q9HW93; O32440;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Methyl-accepting chemotaxis protein PctC;
GN Name=pctC; OrderedLocusNames=PA4307;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9353923; DOI=10.1099/00221287-143-10-3223;
RA Taguchi K., Fukutomi H., Kuroda A., Kato J., Ohtake H.;
RT "Genetic identification of chemotactic transducers for amino acids in
RT Pseudomonas aeruginosa.";
RL Microbiology 143:3223-3229(1997).
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).
RN [3]
RP FUNCTION IN REPELLENT RESPONSES, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16233808; DOI=10.1263/jbb.99.396;
RA Shitashiro M., Tanaka H., Hong C.S., Kuroda A., Takiguchi N., Ohtake H.,
RA Kato J.;
RT "Identification of chemosensory proteins for trichloroethylene in
RT Pseudomonas aeruginosa.";
RL J. Biosci. Bioeng. 99:396-402(2005).
RN [4]
RP FUNCTION, AND DOMAIN.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23650915; DOI=10.1111/mmi.12255;
RA Rico-Jimenez M., Munoz-Martinez F., Garcia-Fontana C., Fernandez M.,
RA Morel B., Ortega A., Ramos J.L., Krell T.;
RT "Paralogous chemoreceptors mediate chemotaxis towards protein amino acids
RT and the non-protein amino acid gamma-aminobutyrate (GABA).";
RL Mol. Microbiol. 88:1230-1243(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27031335; DOI=10.1371/journal.pone.0150109;
RA Schwarzer C., Fischer H., Machen T.E.;
RT "Chemotaxis and binding of Pseudomonas aeruginosa to scratch-wounded human
RT cystic fibrosis airway epithelial cells.";
RL PLoS ONE 11:e0150109-e0150109(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=30425146; DOI=10.1128/mbio.01894-18;
RA Corral-Lugo A., Matilla M.A., Martin-Mora D., Silva Jimenez H.,
RA Mesa Torres N., Kato J., Hida A., Oku S., Conejero-Muriel M., Gavira J.A.,
RA Krell T.;
RT "High-affinity chemotaxis to histamine mediated by the TlpQ chemoreceptor
RT of the human pathogen Pseudomonas aeruginosa.";
RL MBio 9:e01894-e01894(2018).
RN [7] {ECO:0007744|PDB:5LTV}
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 30-281 IN COMPLEX WITH GABA,
RP DOMAIN, AND MOLECULAR EVOLUTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31964737; DOI=10.1128/mbio.03066-19;
RA Gavira J.A., Gumerov V.M., Rico-Jimenez M., Petukh M., Upadhyay A.A.,
RA Ortega A., Matilla M.A., Zhulin I.B., Krell T.;
RT "How bacterial chemoreceptors evolve novel ligand specificities.";
RL MBio 11:e03066-e03066(2020).
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. Responds to L-His, L-Pro and gamma-aminobutyrate (GABA).
CC Also involved in repellent responses to trichloroethylene (TCE),
CC chloroform and methylthiocyanate (PubMed:16233808, PubMed:23650915,
CC PubMed:9353923). Also mediates chemotaxis to histamine, but does not
CC bind histamine (PubMed:30425146). {ECO:0000269|PubMed:16233808,
CC ECO:0000269|PubMed:23650915, ECO:0000269|PubMed:30425146,
CC ECO:0000269|PubMed:9353923}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: The ligand binding region binds directly to 2 L-amino acids
CC (PubMed:23650915). Binding of GABA induces structural changes of the
CC chemoreceptor (PubMed:31964737). {ECO:0000269|PubMed:23650915,
CC ECO:0000269|PubMed:31964737}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows no defect in chemotaxis toward L-
CC amino acids. Mutant shows also decreased chemotactic responses to TCE,
CC chloroform and methylthiocyanate (PubMed:16233808, PubMed:9353923).
CC Deletion of pctA, pctB and pctC abolishes chemotaxis to 5 mM histamine,
CC but significant chemotaxis is observed at a concentration range between
CC 500 nM and 500 uM (PubMed:30425146). The pctABC-tlpQ deletion mutant is
CC devoid of histamine chemotaxis over the entire concentration range (50
CC nM to 50 mM) (PubMed:30425146). The deletion mutant does not show
CC significant reduction in swarming or immobilization near epithelial
CC wounds, but the pctABC triple deletion mutant shows a significant
CC reduction in chemotaxis and immobilization along wounds of human cystic
CC fibrosis airway epithelial cells (PubMed:27031335).
CC {ECO:0000269|PubMed:16233808, ECO:0000269|PubMed:27031335,
CC ECO:0000269|PubMed:30425146, ECO:0000269|PubMed:9353923}.
CC -!- MISCELLANEOUS: PctA has a broad ligand range and responds to most of
CC the proteinogenic amino acids, whereas PctB and PctC have a much
CC narrower range and show strong ligand preference for L-glutamine and
CC gamma-aminobutyrate, respectively. These receptors are paralogs: pctA
CC gene duplication in the common ancestor of the genus Pseudomonas led to
CC pctC, whereas pctB originated through another, independent pctA
CC duplication. {ECO:0000305|PubMed:31964737}.
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; D86947; BAA23410.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07695.1; -; Genomic_DNA.
DR PIR; H83106; H83106.
DR RefSeq; NP_252997.1; NC_002516.2.
DR RefSeq; WP_003148124.1; NZ_CP053028.1.
DR PDB; 5LTV; X-ray; 2.31 A; A/B/C/D/E/F/G=30-281.
DR PDBsum; 5LTV; -.
DR AlphaFoldDB; Q9HW93; -.
DR SMR; Q9HW93; -.
DR STRING; 287.DR97_1482; -.
DR PaxDb; Q9HW93; -.
DR PRIDE; Q9HW93; -.
DR EnsemblBacteria; AAG07695; AAG07695; PA4307.
DR GeneID; 881576; -.
DR KEGG; pae:PA4307; -.
DR PATRIC; fig|208964.12.peg.4510; -.
DR PseudoCAP; PA4307; -.
DR HOGENOM; CLU_000445_107_19_6; -.
DR InParanoid; Q9HW93; -.
DR OMA; YIAHPTI; -.
DR PhylomeDB; Q9HW93; -.
DR BioCyc; PAER208964:G1FZ6-4391-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:0016597; F:amino acid binding; IDA:PseudoCAP.
DR GO; GO:0006935; P:chemotaxis; IMP:PseudoCAP.
DR GO; GO:0043200; P:response to amino acid; IMP:PseudoCAP.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF103190; SSF103190; 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..632
FT /note="Methyl-accepting chemotaxis protein PctC"
FT /id="PRO_0000424851"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..279
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..262
FT /note="Cache"
FT /evidence="ECO:0000255"
FT DOMAIN 301..355
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 360..596
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 408..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000269|PubMed:31964737"
FT BINDING 129..131
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000269|PubMed:31964737"
FT BINDING 150
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000269|PubMed:31964737"
FT BINDING 176
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /evidence="ECO:0000269|PubMed:31964737"
FT CONFLICT 176..177
FT /note="DM -> EW (in Ref. 1; BAA23410)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="A -> D (in Ref. 1; BAA23410)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="S -> C (in Ref. 1; BAA23410)"
FT /evidence="ECO:0000305"
FT HELIX 42..76
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:5LTV"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:5LTV"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5LTV"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:5LTV"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:5LTV"
SQ SEQUENCE 632 AA; 68308 MW; F5A7D3DA33440882 CRC64;
MLRSLSFAKK ILLAAALVVV FAFSCFILYN DYRQREAVRT DTENYLGEIG TLTASNIQSW
LEGRMHLVEG LASQLALLDQ PDEANIARQL EQPVFSRNFA SVYLGEAASG TFTMRPYDAM
PEGYDPRTRA WYKDALAADR LIVTEPFVDA GTGEQILAMS LPVRHAGQLL GVAAGDMKLE
TLTAILNSLK FDGAGYAFLV SDAGKILLHP DSGLVLKTLA EAYPKGAPNI VPGVHEVELD
GSSQFVSFTP VKGLPGVTWY VALVLDRDTA YSMLSEFRTS AIVATLIAVV GIMLLLGMLI
RVLMQPLTDM GRAMQDIAQG EGDLTKRLKV TSNDEFGTLA NAFNRFVERI HESIREVAGT
ARQLHDVAQL VVNASNSSMA NSDEQSNRTN SVAAAINELG AAAQEIARNA ADASHHASDA
NHQAEDGKQV VEQTIRAMNE LSEKISASCA NIEALNSRTV NIGQILEVIK GISEQTNLLA
LNAAIEAARA GEAGRGFAVV ADEVRNLAHR AQESAQQIQK MIEELQVGAR EAVATMTESQ
RYSLESVEIA NRAGERLGSV TSRIGEIDSM NQSVATATEE QTAVVDSLNM DITEINTLNQ
EGVENLQATL RACGELETQA GRLRHLVDSF KI
