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VIRA_AGRFC
ID   VIRA_AGRFC              Reviewed;         833 AA.
AC   P18540; Q52297;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Wide host range VirA protein;
DE            Short=WHR VirA;
DE            EC=2.7.13.3;
GN   Name=virA; OrderedLocusNames=Atu6166; ORFNames=AGR_pTi_2;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OG   Plasmid pTiC58.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2194232; DOI=10.1016/0147-619x(90)90028-b;
RA   Rogowsky P.M., Powell B.S., Shirasu K., Lin T.-S., Morel P., Zyprian E.M.,
RA   Steck T.R., Kado C.I.;
RT   "Molecular characterization of the vir regulon of Agrobacterium
RT   tumefaciens: complete nucleotide sequence and gene organization of the
RT   28.63-kbp regulon cloned as a single unit.";
RL   Plasmid 23:85-106(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Powell G.K.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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; J03320; AAA91590.1; -; Genomic_DNA.
DR   EMBL; L48210; AAA79282.1; -; Genomic_DNA.
DR   EMBL; AE007871; AAK90927.1; -; Genomic_DNA.
DR   PIR; AD3248; AD3248.
DR   PIR; S06972; S06972.
DR   RefSeq; NP_396486.1; NC_003065.3.
DR   RefSeq; WP_010974914.1; NC_003065.3.
DR   AlphaFoldDB; P18540; -.
DR   SMR; P18540; -.
DR   IntAct; P18540; 2.
DR   PRIDE; P18540; -.
DR   EnsemblBacteria; AAK90927; AAK90927; Atu6166.
DR   KEGG; atu:Atu6166; -.
DR   PATRIC; fig|176299.10.peg.5363; -.
DR   HOGENOM; CLU_017728_0_0_5; -.
DR   OMA; QFKSHNA; -.
DR   BioCyc; AGRO:ATU6166-MON; -.
DR   BRENDA; 2.7.13.3; 200.
DR   Proteomes; UP000000813; Plasmid Ti.
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; ISS:PAMGO_GAT.
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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..833
FT                   /note="Wide host range VirA protein"
FT                   /id="PRO_0000074895"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          475..698
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          720..831
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         478
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         770
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   CONFLICT        68
FT                   /note="R -> S (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="L -> V (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="I -> F (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        551
FT                   /note="L -> P (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        655..656
FT                   /note="SC -> CS (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   833 AA;  91322 MW;  B514DAF85BDFB2B5 CRC64;
     MNGRYSPSRQ DFKTGAKPWS ILALVVAAMI FALMAITSWQ DNETNRAILT QLRAINIDSA
     SLQRDVLRAE AGVVANYRPI ISRLGALRKN LENLKRLFKQ SHLVIGNDFS QLLDKLKVSV
     DTTDAAVAAF GAQNVLLQDS LASFTRALSI LPKMSSTDQT VENSNELGSL MLRFVRQPSP
     ALSLEISHEL DMLQKASGGA EVPIRILARE GRVILSILPR VNDAVNMIQT SDTAEIAERL
     ERKCLEAYSL QSVREQRARI FLGSVSVGLC IYIISLVYRL RRKTAWLTRR LDYEEVIKEI
     GVCFEGGGAT ASSLNSSAQA ALGIIQRFFN AESCALALVD HGDRWAVESF AAKLPEPVWE
     DLALREMVSL ARADERASVF RIMSTRKVSC LPPETPGVSM LLAHKSTDQL IAICSLGYQG
     YRLKSCPGEV QLLELATACL CHYIDVRRKQ TECDILERRL EHAERLQAVG TLAGGIAHEF
     NNILGAILGY AEMAQNMLRR SSVTRRHIDQ IISSGDRARL IIDQILTLSR KLERVTKPFS
     VSELVMEIAP LLRVALQRNI ELKFKFDDKK SVVEGSPLEV QQMLMNLCKN ASQAFTADGQ
     IDIIVSRIFV SRQKVLAHGV MPAGDYVLLS VSDDGEGIAE TVLPHIFEPF FTTRSCSGGT
     GLGLAAVHGH VSALAGYIDV TSAVGRGTRF DIYLPPSSKK PVSPDAFFGP CKTPRGNGEI
     VALIEPDPVL REVYEDKIAA LGYEPVGFKT CADLCNWISK GKQADLVLVD QSSLPENQSA
     TALHAAFKTA SIIIGGSDLK MSLSSDDMTS ALFLPKPISS RTMAYAIRTK IKA
 
 
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