PSCA_PSESM
ID PSCA_PSESM Reviewed; 629 AA.
AC Q882Z2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Methyl-accepting chemotaxis protein PscA {ECO:0000305};
DE AltName: Full=PsPto-PscA {ECO:0000303|PubMed:31575767};
GN Name=pscA {ECO:0000303|PubMed:31575767};
GN OrderedLocusNames=PSPTO_2480 {ECO:0000312|EMBL:AAO55987.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=31575767; DOI=10.1128/mbio.01868-19;
RA Cerna-Vargas J.P., Santamaria-Hernando S., Matilla M.A.,
RA Rodriguez-Herva J.J., Daddaoua A., Rodriguez-Palenzuela P., Krell T.,
RA Lopez-Solanilla E.;
RT "Chemoperception of specific amino acids controls phytopathogenicity in
RT Pseudomonas syringae pv. tomato.";
RL MBio 10:e01868-e01868(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. PscA recognizes specifically and with high affinity L-Asp,
CC D-Asp and L-Glu. It exerts a double function, in mediating chemotaxis
CC to these amino acids and in modulating cyclic di-GMP (c-di-GMP) levels,
CC causing alterations in biofilm development. Plays a key role in the
CC infection process. It may facilitate bacterial entry into the plant.
CC {ECO:0000269|PubMed:31575767}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not respond to L-Asp, whereas
CC chemotaxis to D-Asp and L-Glu is significantly reduced. Mutant shows
CC increased c-di-GMP level, a modest but significant increase in biofilm
CC formation and reduced swarming motility. It also shows reduced
CC virulence in tomato plants. {ECO:0000269|PubMed:31575767}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE016853; AAO55987.1; -; Genomic_DNA.
DR RefSeq; NP_792292.1; NC_004578.1.
DR RefSeq; WP_011104030.1; NC_004578.1.
DR STRING; 223283.PSPTO_2480; -.
DR EnsemblBacteria; AAO55987; AAO55987; PSPTO_2480.
DR GeneID; 1184132; -.
DR KEGG; pst:PSPTO_2480; -.
DR PATRIC; fig|223283.9.peg.2519; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_19_6; -.
DR OMA; YIAHPTI; -.
DR OrthoDB; 477199at2; -.
DR PhylomeDB; Q882Z2; -.
DR Proteomes; UP000002515; 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; 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 PRINTS; PR00260; CHEMTRNSDUCR.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..629
FT /note="Methyl-accepting chemotaxis protein PscA"
FT /id="PRO_0000454720"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..276
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 36..258
FT /note="Cache"
FT /evidence="ECO:0000255"
FT DOMAIN 298..352
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 357..593
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ SEQUENCE 629 AA; 67575 MW; 97B07B460C65723E CRC64;
MKNLGFSKKI LLAAALIVVV AFSVFIVIND YRQRQSLKSS VKSELQQLGT LTTQNIQTWL
ESRIQLLQSM SQQVAVDGKE LPQLQRAIGL PTYSDNFQLS YFGSTEGVMF SVPAGNRPAD
YDPRARGWYK AAQNAPGTIV TEPYIAASSG KLVMTIATPV KIQNQLAGVA GADISLDSVS
KIINSLNFDG HGYAFLVSAE GKILVHPDSK LVLKNINEAY PVNTPKIATG VTEIDSGKQP
EIISFTPVQG VATANWYVAL VLEQDSAYAM LTEFRTSAIT AMVVVVMVII LLLGPLIRVL
MQPLHQMGRA MRDIADGEGD LTKRLAITSH DEFGALAESF NHFVERIHTS IREVASTAAQ
LGEVATRVVK VSNASMSNSD QQANRTESVA AAINELGAAA QEIAQNAART SQQSSDASGL
ASDGQGVVQQ TIKAMNELSG KISESCVNIE SLNGKTANIG QILEVITSIS QQTNLLALNA
AIEAARAGEA GRGFAVVADE VRNLAHRTQD SAQQVQKMIE ELQVGAREAV VNMTESQRQS
EDSVGIANLA GERLGSVTRR IEEINGMNQS VAAATEEQTS VVESINVDIT HINTLNQQGV
DNLRQTLEAC NSLEEQAARL QQLVGSFRI
