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   27-MAR-2024, entry version 120.
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; Pseudomonadota; 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: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; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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
//