(data stored in ACNUC7421 zone)

SWISSPROT: Q13EG5_RHOPS

ID   Q13EG5_RHOPS            Unreviewed;      1105 AA.
AC   Q13EG5;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00924638};
DE            EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00924638};
GN   OrderedLocusNames=RPD_0284 {ECO:0000313|EMBL:ABE37524.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37524.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37524.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37524.1,
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; ABE37524.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0284; -.
DR   EnsemblBacteria; ABE37524; ABE37524; RPD_0284.
DR   KEGG; rpd:RPD_0284; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000272524; -.
DR   OMA; MTHEANR; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 2.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; Q13EG5.
DR   SWISS-2DPAGE; Q13EG5.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00908420};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Kinase {ECO:0000256|SAAS:SAAS00924871, ECO:0000313|EMBL:ABE37524.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00908075};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transferase {ECO:0000256|SAAS:SAAS00924820,
KW   ECO:0000313|EMBL:ABE37524.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     39     59       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      376    427       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      443    475       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      516    569       PAC. {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      570    626       PAS. {ECO:0000259|PROSITE:PS50112}.
FT   DOMAIN      711    934       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      955   1071       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   COILED      683    703       {ECO:0000256|SAM:Coils}.
FT   MOD_RES    1005   1005       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   1105 AA;  120476 MW;  9D2767B4108CA89C CRC64;
     MNRPIGQNNY APDTAPDLDS LGPRCPRIEA GAMKLSTRLT LAMVALVLVT TAVLGFLNYR
     SIVELVMPRA LKQLQTHAQL NALLMDAHLR GARADAVGAQ ASSTLRDLLL SRLKTTETPG
     EPAPEWRRRI EARFAAELVA KPTYAILRII GPEDGGRELV RVDRLGPNGG IRAVPVSQLT
     RRGDRSYVRE GLALPRNEVA VSKIELNRNE TGLEIPYVAT MRTMAPIDAP DGTRLGVLVI
     NTNLSENLER VRDSVTRGNL IYIVNAAGDY LLHPDRSREF GFDRGTPSRI QDDFPAFAAL
     LDGKDEAPRV MESSTGQRFG VGWDWVRLAD GPRVGVIEMR SYASLTSVPR AVRDATLTGG
     AAAILVAMLM AVPLARSLTR PLVRITRSVQ AFARGEKFEL TPGGSQEINL LADAFSQMTH
     EANRKAIALA AEVEERTRIA GVLQNTIDIM VDPVLVVDAR GTVILTNPAA CEMFGSLAGI
     SILNTTRSFD RFSPDGKPLT PDKSALLRAF LGETIENFEF IVQPIGSARR SYLTANGRPL
     RGETGQIQGA VMVYHDITKT KKAEEALRRS EQMARAIVDT ALDAFVQVDA LGTITEWSPH
     AELVLGWRRS EAIGRNVFQL LIPADQLERR TEEFKRFASS LGRDSSGFRV EIEVLHQDGT
     PTPIEVAMTA LYRDGSFVIN AFLRNLTEQI AFEEQLRQSQ KMESIGQLTG GIAHDFNNML
     TVITGTIDII SDGVADQPHL ATIAKLISEA ADRGAELTRL LLAFARKQPL RPDETDVNAL
     VAGLQSLLRP TLGEQIEIET SFDDGAWPIY VDRGQLESAL VNLAVNARDA MPNGGKLTIE
     TCNIVVDQEL AKRFGNVESG SYVMIAISDS GCGIPDAIRG KVFDPFFTTK EVGKGTGLGL
     SMVYGFIKQS GGHITLYSEV GLGTTFRLYL PRASTENERE AATSSEQGAV GGTETILVVE
     DDAMVRSYVN AQLKSLGYTA LSVGNATAAL SISDSGAEFD LLFTDVVMPG PYNGVQLAAE
     MSKRRPGLKV LFTSGYSENA LIYNDRLDPD ILLLSKPYRR ADLARMIRLA LNSTVESEVI
     QNAADEHLKN ERVDDNVERS SVRPL
//

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