HRC2_XANEU
ID HRC2_XANEU Reviewed; 645 AA.
AC P80150;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein hrpC2;
GN Name=hrpC2;
OS Xanthomonas euvesicatoria.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=456327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 75-3;
RX PubMed=1472717; DOI=10.1094/mpmi-5-390;
RA Fenselau S., Balbo I., Bonas U.;
RT "Determinants of pathogenicity in Xanthomonas campestris pv. vesicatoria
RT are related to proteins involved in secretion in bacterial pathogens of
RT animals.";
RL Mol. Plant Microbe Interact. 5:390-396(1992).
CC -!- FUNCTION: Involved in the secretion of a proteinaceous elicitor of the
CC hypersensitivity response in plants. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export
CC pore) family. {ECO:0000305}.
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DR EMBL; M99176; AAA27606.1; -; Genomic_DNA.
DR RefSeq; WP_046934829.1; NZ_JTEJ01000161.1.
DR AlphaFoldDB; P80150; -.
DR SMR; P80150; -.
DR PATRIC; fig|456327.29.peg.3437; -.
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:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 1.10.8.540; -; 1.
DR Gene3D; 3.40.30.60; -; 1.
DR Gene3D; 3.40.50.12790; -; 1.
DR InterPro; IPR042194; FHIPEP_1.
DR InterPro; IPR042193; FHIPEP_3.
DR InterPro; IPR042196; FHIPEP_4.
DR InterPro; IPR025505; FHIPEP_CS.
DR InterPro; IPR001712; T3SS_FHIPEP.
DR PANTHER; PTHR30161; PTHR30161; 2.
DR Pfam; PF00771; FHIPEP; 2.
DR PIRSF; PIRSF005419; FlhA; 1.
DR PRINTS; PR00949; TYPE3IMAPROT.
DR PROSITE; PS00994; FHIPEP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hypersensitive response elicitation;
KW Membrane; Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..645
FT /note="Protein hrpC2"
FT /id="PRO_0000190023"
FT TRANSMEM 18..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 69876 MW; CBF9CB63067E74BB CRC64;
MLGDRVRATR YFAYSGEVAI AALVVAVIGL MILPLPTPMI DTLLGINITL SVVLLMVTMY
VPDSISLSSF PSLLLFTTLL RLSLNIASTK SILLHAEAGH IIESFGELVV GGNLVVGLVV
FLIITTVQFI VIAKGSERVA EVGARFTLDA MPGKQMSIDA DLRGGNLTAD EARRKRARLA
MESQLHGGMD GAMKFVKGDA IAGLVITMVN ILAGIVVGVT YHGMTAGDAA NRFAILSVGD
AMVSQIASLL ISVAAGVMIT RVANENETRL SSLGLDIGRQ LTSNARALMA ASVLLACFAF
VPGFPAVLFL LLAAAVGAGG YTIWRKQRDI SGTDQRKLPS ASRKGAKGEA PHIRKNAPDF
ASPLSMRLSP QLAALLDPAR LDQAIESERR QLVELLGLPF PGIAIWQTES LQGMQYEVLI
HDVPETRAEL ENTDDMQAAL ARQAISPLHA RAHLFVGIQE TQWMLEQVAV DYPGLVAEVN
KAMPAQRIAD VLRRLLEERI PVRNIKSILE SLVVWGPKEK DLLMLTEYVR CDLGRYLAHT
ATAGTGQLPA VMLDHAVEQL IRQSIRATAA GNFLALPPEQ ANQLVEQVER IVGDHAQHPL
AVVASMDVRR YVRRMIEARL TWLQVYSFQE LGSEVQLQPI GRVVV