ID   VIRAW_RHIRD             Reviewed;         829 AA.
AC   P07168;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Wide host range VirA protein;
DE            Short=WHR VirA;
DE            EC=2.7.13.3;
GN   Name=virA;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OG   Plasmid pTiA6.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A348, and A856;
RX   PubMed=3595559; DOI=10.1002/j.1460-2075.1987.tb04830.x;
RA   Leroux B., Yanofsky M.F., Winans S.C., Ward J.E., Ziegler S.F.,
RA   Nester E.W.;
RT   "Characterization of the virA locus of Agrobacterium tumefaciens: a
RT   transcriptional regulator and host range determinant.";
RL   EMBO J. 6:849-856(1987).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; X05240; CAA28867.1; -; Genomic_DNA.
DR   PIR; B27211; B27211.
DR   AlphaFoldDB; P07168; -.
DR   SMR; P07168; -.
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: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   3: Inferred from homology;
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_0000074896"
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;  91798 MW;  8991B52AFEB72D5C CRC64;
     MNGRYSPTRQ DFKTGAKPWS ILALIVAAMI FAFMAVASWQ DNATTQAILS QLRSINADSA
     SLQRDVARAH TGTGRNYRPI ISRLGALRKN LEDLKQLFRQ SHIVSESNAA QLLRQLEVSL
     NSADAAVRAF GAQNVRLQDS LASFTRALSS LPGKASTDQT LEKPTELASM MLQFLRQPSP
     AISFEISLEL ERLQKQRGLD EAPVRILARE GPIILSLLPQ VKDLVNMIQT SDTAEIAEML
     QRECLEVYSL KNVEERSARI FLGSASVGLC LYIITLVYRL RKKTDWLARR LDYEELIKEI
     GVCFEGEAAT TSSAQAALRI IQRFFDADTC ALRLVDHDRR WAVETFGAKH PKPVWDDSVL
     REIVSRTKAD ERATVFRIIS SKKIVHLPLE IPGLSILLAH KSTDKLIAVC SLGYQSYRPR
     PCQGEIQLLE LATACLCHYI DVRRKQTECD VLARRLEHAQ RLEAVGTLAG GIAHEFNNIL
     GSILGHAELA QNSVSRTSVT RRYIDYIISS GDRAMLIIDQ ILTLSRKQER MIKPFSVSEL
     VTEIAPLLRM ALPPNIELSF RFDQMQSVIE GSPLELQQVL INICKNASQA MTANGQIDII
     ISQAFLPVKK ILAHGVMPPG DYVLLSISDN GGGIPEAVLP HIFEPFFSTR ARNGGTGLGL
     ASVHGHISAF AGYIDVSSTV GHGTRFDIYL PPSSKEPVNP DSFFGRNKAP RGNGEIVALV
     EPDDLLREAY EDKIAALGYE PVGFRTFNEI RDWISKGNEA DLVMVDQASL PEDQSPNSVD
     LVLKTSAIII GGNDLKMTLS REDVTRDLYL PKPISSRTMA HAILTKIKT