(data stored in SCRATCH zone)

SWISSPROT: Q13EY0_RHOPS

ID   Q13EY0_RHOPS            Unreviewed;       909 AA.
AC   Q13EY0;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00924638};
DE            EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00924638};
GN   OrderedLocusNames=RPD_0119 {ECO:0000313|EMBL:ABE37359.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37359.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37359.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37359.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
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DR   EMBL; CP000283; ABE37359.1; -; Genomic_DNA.
DR   RefSeq; WP_011500552.1; NC_007958.1.
DR   STRING; 316057.RPD_0119; -.
DR   EnsemblBacteria; ABE37359; ABE37359; RPD_0119.
DR   KEGG; rpd:RPD_0119; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000272524; -.
DR   OMA; VAFIENN; -.
DR   OrthoDB; 1755994at2; -.
DR   BioCyc; RPAL316057:RPD_RS00600-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; Q13EY0.
DR   SWISS-2DPAGE; Q13EY0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Kinase {ECO:0000256|SAAS:SAAS00924871, ECO:0000313|EMBL:ABE37359.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transferase {ECO:0000256|SAAS:SAAS00924820}.
FT   DOMAIN      341    392       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      397    433       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      475    528       PAC. {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      541    764       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      784    900       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   MOD_RES     834    834       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   909 AA;  97248 MW;  FCFA0831A9CD0483 CRC64;
     MRLSMRLTLV MTTLVLCAVA AVGILTYYNV GRAVVPAGLT RLADRAEARL GAFDGILRLL
     QLEILAARTF PPHQGLVRAR INGGLDPQDD LTEARWLRRL GDAYLGQMSV KSDIVRFSLV
     SADGGRELLR VDRSGPGGDI RVVPDDKLER VGQELFDRTI ALSEGEVYTS PIHAGPGNSG
     DDDLAPMVSI ATPLRMPEGE PFGMLVLDFD LRPTFERIRA SPDNNTKAYF VDAGGPYLLD
     LLDGRVIPSR PRGQWQDDYP DLAKALGDKP GAATVLTAPD GARVAAAIAI APLVGRLRVG
     VIETEAFERI IAPATALRQT VVTVALFAAG VAVLLSALLS RSLAKPLVQI TAAVDDFAST
     GRVAMPRGLS GETKTLAAAF EHMAAEIDTT TTALRAKSEA LDKIVASMAD AVLMLDAEGR
     RVFANPTFFA LFGDIAEIGS ERWRQHYQGL RPDGVTPIPD DETPSARARR GESFDNLDVV
     LRRVGHSQLV HLAASGRPIE TASGAFDGAV VVYRNVTALK ETERQLRQAQ KMQAIGQLTG
     GVAHDLNNIL TVLTGGIEIL ADGVSDRPAL KDVAVMVDQA VSRASDLTNG LLSFARKQPL
     QPRSIDVNAL MQETARLLRA TFGSHIEIAF EPTPGLRSAL ADPSQLSGAL INLAINARDA
     MPGGGKLLLE AGNIDLDQAY ADHNDEVAAG RYVVLMVTDT GTGIPAAIRD RVFEPFFTTK
     ALGEGTGLGL SMVYGFVKQS GGHIAIYSEE GVGTTIRLYL PSADPKNSPG DAAAPQQAQG
     GRESILLIED DVLVRSYVVT DLAALGYTVH AAATAAQAMA MVYDELEFDL LFTDVMLAGS
     INGYQLADEL RKYRPDLKVL LTSGYTGNML RLQGGHEDGT PFLEKPYRRA ELARMLRLAL
     DGKAPSSPT
//

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