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CTPM_PSEAE
ID   CTPM_PSEAE              Reviewed;         561 AA.
AC   Q9I0I6;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Methyl-accepting chemotaxis protein CtpM {ECO:0000305};
GN   Name=ctpM {ECO:0000305}; OrderedLocusNames=PA2652;
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=17933940; DOI=10.1128/aem.01898-07;
RA   Alvarez-Ortega C., Harwood C.S.;
RT   "Identification of a malate chemoreceptor in Pseudomonas aeruginosa by
RT   screening for chemotaxis defects in an energy taxis-deficient mutant.";
RL   Appl. Environ. Microbiol. 73:7793-7795(2007).
RN   [3]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=29391435; DOI=10.1038/s41598-018-20283-7;
RA   Martin-Mora D., Ortega A., Perez-Maldonado F.J., Krell T., Matilla M.A.;
RT   "The activity of the C4-dicarboxylic acid chemoreceptor of Pseudomonas
RT   aeruginosa is controlled by chemoattractants and antagonists.";
RL   Sci. Rep. 8:2102-2102(2018).
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 (Probable). Directly recognizes five C4-dicarboxylic acids:
CC       L-malic, citramalic, citraconic, bromosuccinic and methylsuccinic acids
CC       (PubMed:17933940, PubMed:29391435). Three of the identified ligands act
CC       as chemoattractants (L-malic, D,L-bromosuccinic and L-citramalic acids)
CC       whereas two of them (L-methylsuccinic and citraconic acids) behave as
CC       antagonists by inhibiting the downstream chemotaxis signaling cascade
CC       (PubMed:29391435). Antagonists compete with chemoattractants, thereby
CC       decreasing the affinity for chemoattractants and the subsequent
CC       chemotactic response (PubMed:29391435). Acts through the che
CC       chemosensory pathway (PubMed:29391435). {ECO:0000269|PubMed:17933940,
CC       ECO:0000269|PubMed:29391435, ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. The ligand-binding domain (LBD) is dimeric in the
CC       presence and the absence of ligands. {ECO:0000269|PubMed:29391435}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Mutant shows a dramatic reduction in chemotaxis
CC       for all ligands, but it does not affect response to casamino acids
CC       (PubMed:29391435). Mutant showed no attraction to malate at any of the
CC       concentrations tested (PubMed:17933940). Mutation does not affect plant
CC       root colonization (PubMed:29391435). {ECO:0000269|PubMed:17933940,
CC       ECO:0000269|PubMed:29391435}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG06040.1; -; Genomic_DNA.
DR   PIR; G83313; G83313.
DR   RefSeq; NP_251342.1; NC_002516.2.
DR   RefSeq; WP_010895628.1; NZ_QZGE01000008.1.
DR   AlphaFoldDB; Q9I0I6; -.
DR   SMR; Q9I0I6; -.
DR   STRING; 287.DR97_5309; -.
DR   PaxDb; Q9I0I6; -.
DR   PRIDE; Q9I0I6; -.
DR   EnsemblBacteria; AAG06040; AAG06040; PA2652.
DR   GeneID; 882361; -.
DR   KEGG; pae:PA2652; -.
DR   PATRIC; fig|208964.12.peg.2775; -.
DR   PseudoCAP; PA2652; -.
DR   HOGENOM; CLU_000445_107_27_6; -.
DR   InParanoid; Q9I0I6; -.
DR   OMA; DNVVNTM; -.
DR   PhylomeDB; Q9I0I6; -.
DR   BioCyc; PAER208964:G1FZ6-2692-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:0071310; P:cellular response to organic substance; IMP:PseudoCAP.
DR   GO; GO:0006935; P:chemotaxis; IMP:PseudoCAP.
DR   GO; GO:0050918; P:positive chemotaxis; IMP:PseudoCAP.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM01049; Cache_2; 1.
DR   SMART; SM00304; HAMP; 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   Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..561
FT                   /note="Methyl-accepting chemotaxis protein CtpM"
FT                   /id="PRO_0000424880"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..205
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          230..284
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          289..525
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT   REGION          333..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  60344 MW;  2C7DC692B37278BC CRC64;
     MMRLTLKSKV LLLAMVPVLL FALVLSGGAV LILKKQADAE VKDTRERLLG DRRAELEHYV
     QIAMGSIQAE YDRSANGDLN ARAEAIARLS KIKYGKDGYI FGYDSQVVRL FRGDSPVDVG
     KSFRDRRDPS GVYLNRELVE AGRNGSHYVT YTSPLPGNES VMVPKLSYTL YLPKWDMVIG
     SAINLDGVEA QLVEIKQDID ERIGTLIASI VGIAGVLLVV LLVIGLAVAN AMLRPLHQIR
     QNLDDIAAGE GDLTRRLPVT SYDELGELAG SFNRFVEKIH GLVRQIAGMT GDLKQLVEQM
     SAQAERSEQA MERQRHETDQ VATAINEMSA AAHEVAQSAQ RAAEAAQQTD HEGQAAKRVV
     DGSIERIHAL VDEIRDSGTS LDSLQQDVQS IVSVLGVIRS IAEQTNLLAL NAAIEAARAG
     EAGRGFAVVA DEVRALASRT QQSTQEIQGM IDRLQQGTNA AVDAMRRSGE AGEGTSNQAN
     QAGDSLDAIA QLIATINAMN AQIASAAEEQ TAVAEEINRS VHQIAGAVDS VADEAQQGAQ
     TARSLAQLGQ GLGRLVGQFR I
 
 
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