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HPAB3_PSEYM
ID   HPAB3_PSEYM             Reviewed;         385 AA.
AC   Q8RP04;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Effector protein hopAB3;
DE   AltName: Full=Avirulence protein hopPmaL;
GN   Name=hopAB3; Synonyms=hopPmaL;
OS   Pseudomonas syringae pv. maculicola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=59511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ES4326;
RX   PubMed=11872842; DOI=10.1126/science.295.5560.1722;
RA   Guttman D.S., Vinatzer B.A., Sarkar S.F., Ranall M.V., Kettler G.,
RA   Greenberg J.T.;
RT   "A functional screen for the type III (Hrp) secretome of the plant pathogen
RT   Pseudomonas syringae.";
RL   Science 295:1722-1726(2002).
RN   [2]
RP   FUNCTION IN VIRULENCE AND AVIRULENCE, AND SUBCELLULAR LOCATION.
RC   STRAIN=ES4326;
RX   PubMed=16391110; DOI=10.1128/aem.72.1.702-712.2006;
RA   Lin N.-C., Abramovitch R.B., Kim Y.-J., Martin G.B.;
RT   "Diverse AvrPtoB homologs from several Pseudomonas syringae pathovars
RT   elicit Pto-dependent resistance and have similar virulence activities.";
RL   Appl. Environ. Microbiol. 72:702-712(2006).
CC   -!- FUNCTION: Effector protein involved in gene-for-gene resistance in
CC       tomato plants. It is recognized by the host Pto resistance protein and
CC       elicits Pto and Prf-dependent hypersensitive response (HR) and
CC       programmed cell death (PCD), resulting in host immunity. In susceptible
CC       plants, promotes virulence, in part, by enhancing the development of
CC       disease symptoms and bacterial growth. {ECO:0000269|PubMed:16391110}.
CC   -!- SUBUNIT: Interacts physically with plant cell Pto.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16391110}.
CC       Note=Secreted via type III secretion system (TTSS). Localized to the
CC       plant cell cytoplasm.
CC   -!- MISCELLANEOUS: Unlike other effector proteins from the HopAB family,
CC       lacks the anti-PCD region and cannot inhibit cell death triggered by
CC       AvrPto/Pto.
CC   -!- SIMILARITY: Belongs to the HopAB family. {ECO:0000305}.
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DR   EMBL; AF458050; AAL84252.1; -; Genomic_DNA.
DR   PDB; 2LF3; NMR; -; A=281-385.
DR   PDB; 3TJY; X-ray; 1.70 A; A=140-233.
DR   PDBsum; 2LF3; -.
DR   PDBsum; 3TJY; -.
DR   AlphaFoldDB; Q8RP04; -.
DR   BMRB; Q8RP04; -.
DR   SMR; Q8RP04; -.
DR   EvolutionaryTrace; Q8RP04; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR   CDD; cd12803; HopAB_BID; 1.
DR   CDD; cd12802; HopAB_PID; 1.
DR   Gene3D; 1.20.1280.220; -; 1.
DR   InterPro; IPR031759; HopAB_BAK-bd.
DR   InterPro; IPR038342; HopAB_BAK-bd_sf.
DR   InterPro; IPR033743; HopAB_PID.
DR   Pfam; PF16847; AvrPtoB_bdg; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hypersensitive response elicitation; Secreted; Virulence.
FT   CHAIN           1..385
FT                   /note="Effector protein hopAB3"
FT                   /id="PRO_0000234083"
FT   REGION          1..333
FT                   /note="Host recognition"
FT                   /evidence="ECO:0000250"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           142..155
FT                   /evidence="ECO:0007829|PDB:3TJY"
FT   HELIX           160..171
FT                   /evidence="ECO:0007829|PDB:3TJY"
FT   HELIX           180..189
FT                   /evidence="ECO:0007829|PDB:3TJY"
FT   HELIX           193..196
FT                   /evidence="ECO:0007829|PDB:3TJY"
FT   HELIX           203..216
FT                   /evidence="ECO:0007829|PDB:3TJY"
FT   HELIX           301..304
FT                   /evidence="ECO:0007829|PDB:2LF3"
FT   HELIX           309..322
FT                   /evidence="ECO:0007829|PDB:2LF3"
FT   HELIX           326..337
FT                   /evidence="ECO:0007829|PDB:2LF3"
FT   HELIX           345..353
FT                   /evidence="ECO:0007829|PDB:2LF3"
FT   TURN            363..368
FT                   /evidence="ECO:0007829|PDB:2LF3"
FT   HELIX           371..384
FT                   /evidence="ECO:0007829|PDB:2LF3"
SQ   SEQUENCE   385 AA;  41628 MW;  64E0E164796BE7D8 CRC64;
     MVGISGRAGP SGSYNYSGHT DNPEPVSGRA RDSNSEANSS NSPQVPPPLN APASPMPAGR
     PRFLRSMALS SQTREWLEKG MPTEAEAGVP IRLQERAANT APQARAEERH TQPADAAAPH
     ARAERGRTLQ APASTSPLYT GAVPRANRIV QQLVEAGADL ANIRTMFRNM LRGEEMILSR
     AEQNVFLQHF PDMLPCGIDR NSELAIALRE ALRRADSQQA ARAPARTPPR SSVRTPERSP
     APRTATESSS GSNQRSLLGR FAGLMTSNQR RPSSASNAST SQRPVDRNPP RINLMPTGAN
     RVAMRNRGNN EADAALQALA QNGINMEDLR AALEAYIVWL RPIPLDIANA LEGVGITPRF
     DNPEEAKVDN PLMNLSSALK RRLDA
 
 
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