VIRA_AGRT9
ID VIRA_AGRT9 Reviewed; 829 AA.
AC P10799;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Wide host range VirA protein;
DE Short=WHR VirA;
DE EC=2.7.13.3;
GN Name=virA;
OS Agrobacterium tumefaciens (strain 15955).
OG Plasmid pTi15955.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=190386;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND92000074; DOI=10.1007/BF00015676;
RA Melchers L.S., Thompson D.V., Idler K.B., Neuteboom S.T.C., Maagd R.A.,
RA Schilperoort R.A., Hooykaas P.J.J.;
RT "Molecular characterization of the virulence gene virA of the Agrobacterium
RT tumefaciens octopine Ti plasmid.";
RL Plant Mol. Biol. 11:227-237(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2796735; DOI=10.1111/j.1365-2958.1989.tb00274.x;
RA Morel P., Powell B.S., Rogowsky P.M., Kado C.I.;
RT "Characterization of the virA virulence gene of the nopaline plasmid,
RT pTiC58, of Agrobacterium tumefaciens.";
RL Mol. Microbiol. 3:1237-1246(1989).
CC -!- FUNCTION: Activates VirG, by phosphorylating it, in the presence of
CC acetosyringone or hydroxysyringone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- INTERACTION:
CC P10799; P10799: virA; NbExp=2; IntAct=EBI-6452433, EBI-6452433;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; X16905; CAA34777.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P10799; -.
DR SMR; P10799; -.
DR BRENDA; 2.7.13.3; 200.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR045812; DAHL.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF19443; DAHL; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Crown gall tumor; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plasmid; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..829
FT /note="Wide host range VirA protein"
FT /id="PRO_0000074897"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 471..694
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 716..827
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 474
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 766
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 829 AA; 91640 MW; 9D1150B84A889809 CRC64;
MNGRYSPTRQ DFKTGAKPWS ILALIVAAMI FAFMAVASWQ DNATTQAILS QLRSINADSA
SLQRDVLRAH TGTVANYRPI ISRLGALRKN LEDLKQLFRQ SHIVSESNAA QLLRQLEVSL
NSADAAVAAF GAQNVRLQDS LASFTRALSS LPGKASTDQT LEKPTELASM MLQFLRQPSP
AISFEISLEL ERLQKQRGLD EAPVRILARE GPIILSLLPQ VKDLVNMIQT SDTAEIAEML
QRECLEVYSL KNVEERSARI FLGSASVGLC LYIITLVYRL RKKTDWLARR LDYEELIKEI
GVCFEGEAAT TSSAQAALRI IQRFFDADTC ALALVDHDRR WAVETFGAKH PKPVWDDSVL
REIVSRTKAD ERATVFRIIS SKKIVHLPLE IPGLSILLAH KSTDKLIAVC SLGYQSYRPR
PCQGEIQLLE LATACLCHYI DVRRKQTQCD VLARRLEHAQ RLEAVGTLAG GIAHEFNNIL
GSILGHAELA QNSVSRTSVT RRYIDYIISS GDRAMLIIDQ ILTLSRKQER MIKPFSVSEL
VTEIAPLLRM ALPPNIELSF RFDQMQSVIE GSPLELQQVL INICKNASQA MTANGQIDII
ISQAFLPVKK ILAHGVMPPG DYVLLSISDN GGGIPEAVLP HIFEPFFTTR ARNGGTGLGL
ASVHGHISAF AGYIDVSSTV GHGTRFDIYL PPSSKEPVNP DSFFGRNKAP RGNGEIVALV
EPDDLLREAY EDKIAALGYE PVGFRTFNEI RDWISKGNEA DLVMVDQASL PEDQSPNSVD
LVLKTASIII GGNDLKMTLS REDVTRDLYL PKPISSRTMA HAILTKIKT