HPAB1_PSE14
ID HPAB1_PSE14 Reviewed; 539 AA.
AC Q48B61;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Effector protein hopAB1;
GN Name=hopAB1; Synonyms=virPphA; OrderedLocusNames=PSPPH_A0127;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OG Plasmid large.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
RN [2]
RP SUBCELLULAR LOCATION, AND INDUCTION BY HRPL.
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).
CC -!- FUNCTION: Effector protein that plays different roles depending on the
CC species and plant cultivars that interact with the pathogen. Acts as a
CC virulence determinant by enhancing the development of disease symptoms
CC and bacterial growth. Acts as an avirulence factor by eliciting
CC hypersensitive response (HR) and plant resistance (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15553250}.
CC Note=Secreted via type III secretion system (TTSS).
CC -!- INDUCTION: Transcriptionally induced by HrpL.
CC {ECO:0000269|PubMed:15553250}.
CC -!- SIMILARITY: Belongs to the HopAB family. {ECO:0000305}.
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DR EMBL; CP000059; AAZ37972.1; -; Genomic_DNA.
DR RefSeq; WP_011282445.1; NC_007274.1.
DR PDB; 2LF6; NMR; -; A=220-320.
DR PDBsum; 2LF6; -.
DR AlphaFoldDB; Q48B61; -.
DR BMRB; Q48B61; -.
DR SMR; Q48B61; -.
DR STRING; 264730.PSPPH_A0127; -.
DR EnsemblBacteria; AAZ37972; AAZ37972; PSPPH_A0127.
DR KEGG; psp:PSPPH_A0127; -.
DR eggNOG; ENOG5030NBE; Bacteria.
DR HOGENOM; CLU_505137_0_0_6; -.
DR OMA; TSCLFGE; -.
DR OrthoDB; 2112897at2; -.
DR Proteomes; UP000000551; Plasmid large.
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 Gene3D; 3.30.40.110; -; 1.
DR InterPro; IPR015133; E3_ubiquit_lig_AvrPtoB.
DR InterPro; IPR031759; HopAB_BAK-bd.
DR InterPro; IPR038342; HopAB_BAK-bd_sf.
DR InterPro; IPR038448; HopAB_E3_ubiquit_lig_sf.
DR InterPro; IPR033743; HopAB_PID.
DR Pfam; PF09046; AvrPtoB-E3_ubiq; 1.
DR Pfam; PF16847; AvrPtoB_bdg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hypersensitive response elicitation; Plasmid; Secreted;
KW Virulence.
FT CHAIN 1..539
FT /note="Effector protein hopAB1"
FT /id="PRO_0000236790"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2LF6"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:2LF6"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:2LF6"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2LF6"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:2LF6"
FT TURN 292..297
FT /evidence="ECO:0007829|PDB:2LF6"
FT HELIX 301..315
FT /evidence="ECO:0007829|PDB:2LF6"
SQ SEQUENCE 539 AA; 59575 MW; 9755A3F3770319C6 CRC64;
MPGINGAGPS NFFWQWRTDG EPVTEREHDS SRSASSANSP ELPPPASPAE SGRQRLLRSS
ALSRQTREWL EATPARVQGA TPPAEARQSP EAQQAERIVQ ELVRGGADLN NVRTMLRNVM
DNNAVAFSRV ERDILLQHFP NMPMTGISSD SVLANELRQR LRQTVRQQRI QSSTPARLAD
SSSGSSQRSL IGRSTMLMTP GRSSSSSAAA SRTSVDRHPQ GLDLESARLA SAARHNHSAN
QTNEALRRLT QEGVDMERLR TSLGRYIMSL EPLPPDLRRA LESVGINPFI PEELSLVDHP
VLNFSAALNR MLASRQTTTN SPELPPLASS AESGRRRLLR SPPLLSGQRE WIEQSMRQEA
EPQSSRLNRA VRLAVMPPQN ENEDNVAYAI RLRRLNPGAD VSRVVASFIT DPAARQQVVN
DIRAALDIAP QFSQLRTISK ADAESEELGF RDAADHPDNA TSCLFGEELS LSNPDQQVIG
LAVNPTDKPQ PYSQEVNKAL TFMDMKKLAQ YLADKPEHPL NRQRLDAKNI AKYAFKIVP
