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HRPZ_PSESH
ID   HRPZ_PSESH              Reviewed;         345 AA.
AC   Q9F0B0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Harpin HrpZ;
DE   AltName: Full=Harpin-Psph;
DE   AltName: Full=HrpZ-Psph protein;
GN   Name=hrpZ;
OS   Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS   phaseolicola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=1302A / Race 6;
RX   PubMed=11134504; DOI=10.1073/pnas.98.1.289;
RA   Lee J., Kluesener B., Tsiamis G., Stevens C., Neyt C., Tampakaki A.P.,
RA   Panopoulos N.J., Noeller J., Weiler E.W., Cornelis G.R., Mansfield J.W.,
RA   Nuernberger T.;
RT   "HrpZPsph from the plant pathogen Pseudomonas syringae pv. phaseolicola
RT   binds to lipid bilayers and forms an ion-conducting pore in vitro.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:289-294(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1302A / Race 6;
RX   AGRICOLA=IND43617657; DOI=10.1111/j.1364-3703.2004.00212.x;
RA   Gropp S.J., Guttman D.S.;
RT   "The PCR amplification and characterization of entire Pseudomonas syringae
RT   hrp/hrc clusters.";
RL   Mol. Plant Pathol. 5:137-140(2004).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=NPS 3121;
RX   PubMed=11106029; DOI=10.1094/mpmi.2000.13.12.1366;
RA   Tampakaki A.P., Panopoulos N.J.;
RT   "Elicitation of hypersensitive cell death by extracellularly targeted
RT   HrpZPsph produced in planta.";
RL   Mol. Plant Microbe Interact. 13:1366-1374(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=11340183; DOI=10.2307/3871365;
RA   Lee J., Klessig D.F., Nuernberger T.;
RT   "A harpin binding site in tobacco plasma membranes mediates activation of
RT   the pathogenesis-related gene HIN1 independent of extracellular calcium but
RT   dependent on mitogen-activated protein kinase activity.";
RL   Plant Cell 13:1079-1093(2001).
RN   [5]
RP   TRANSCRIPTIONAL REGULATION.
RC   STRAIN=1449B / Race 7, and 1488A / Race 7;
RX   PubMed=15553250; DOI=10.1094/mpmi.2004.17.11.1250;
RA   Thwaites R., Spanu P.D., Panopoulos N.J., Stevens C., Mansfield J.W.;
RT   "Transcriptional regulation of components of the type III secretion system
RT   and effectors in Pseudomonas syringae pv. phaseolicola.";
RL   Mol. Plant Microbe Interact. 17:1250-1258(2004).
RN   [6]
RP   FUNCTION.
RC   STRAIN=Race 6;
RX   PubMed=15672819; DOI=10.1094/mpmi-18-0060;
RA   Li C.-M., Haapalainen M., Lee J., Nuernberger T., Romantschuk M., Taira S.;
RT   "Harpin of Pseudomonas syringae pv. phaseolicola harbors a protein binding
RT   site.";
RL   Mol. Plant Microbe Interact. 18:60-66(2005).
CC   -!- FUNCTION: Harpins are proteins able to elicit hypersensitive response
CC       (HR) in non-host plants and are required for pathogenicity in host
CC       plants. HrpZ forms ion-conducting pores permeable for cations. Such
CC       pore-forming activity may allow nutrient release and/or delivery of
CC       virulence factors during bacterial colonization of host plants. Also
CC       binds peptides, which contain tryptophan and leucine, suggesting a
CC       protein-protein interaction between the harpin and a host plant
CC       protein, possibly involved in the bacterial pathogenesis.
CC       {ECO:0000269|PubMed:11106029, ECO:0000269|PubMed:11340183,
CC       ECO:0000269|PubMed:15672819}.
CC   -!- SUBUNIT: Homomultimeric. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
CC       Note=Secreted via type III secretion system (TTSS), delivered into the
CC       host intercellular space. HrpZ travels through the hrp pilus and it is
CC       secreted only from the pilus tip (By similarity). It is found to
CC       associate stably with liposomes and synthetic bilayer membranes.
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expression enhanced by contact with host cell wall. Also
CC       regulated by HrpRS and HrpL. {ECO:0000269|PubMed:15553250}.
CC   -!- DOMAIN: The glycine-rich region is characteristic of harpins.
CC   -!- SIMILARITY: Belongs to the harpin HrpZ family. {ECO:0000305}.
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DR   EMBL; AF268940; AAF99292.1; -; Genomic_DNA.
DR   EMBL; AY530203; AAS20457.1; -; Genomic_DNA.
DR   RefSeq; WP_011167991.1; NZ_RBTC01000005.1.
DR   AlphaFoldDB; Q9F0B0; -.
DR   PATRIC; fig|319.14.peg.1560; -.
DR   OMA; MDDNPAQ; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR   InterPro; IPR006961; HrpN/Z.
DR   Pfam; PF04877; Harpin; 1.
PE   2: Evidence at transcript level;
KW   Host cell membrane; Host membrane; Hypersensitive response elicitation;
KW   Ion channel; Ion transport; Membrane; Repeat; Secreted; Transport;
KW   Virulence.
FT   CHAIN           1..345
FT                   /note="Harpin HrpZ"
FT                   /id="PRO_0000220300"
FT   REPEAT          213..219
FT                   /note="1-1"
FT   REPEAT          269..275
FT                   /note="1-2"
FT   REGION          86..194
FT                   /note="Peptide-binding"
FT   REGION          202..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..275
FT                   /note="2 X 7 AA repeats of G-G-G-L-G-[ST]-P"
FT   COMPBIAS        215..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  35250 MW;  A4B0B23A67268CA2 CRC64;
     MQSLSLNSST LQSPSMALVL IRPETETTGS STSSRALQEV IAQLAQELTH NGQLDESSPL
     GKLLGKAMAA SGKAGGGLED IKAALDTLIH EKLGDNFGAS ADNASDTGQH DLMTQVLNGL
     AKSMLNDLLT KQDDGTRFSE DDMPMLKKIA EFMDDNPAQF PKPDSGSWVN ELKEDNFLDG
     DETAQFRSAL DIIGQQLGSQ QNAAGGLAGD SSGGGLGSPV SNTENSPGSL GDPLIDANTG
     PASNSNSNGD VGQLIGELID RGLQSVLAGG GLGTPVSTAN TALVPGGEQP NQDLGQLLGG
     LLQKGLEATL QDAGQTGTGV QSSAAQVALL LVNMLLQSTK NQAAA
 
 
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