ID Q07H02_RHOP5 Unreviewed; 723 AA.
AC Q07H02;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RPE_4863 {ECO:0000313|EMBL:ABJ08782.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ08782.1};
RN [1] {ECO:0000313|EMBL:ABJ08782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ08782.1};
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., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-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; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP000463; ABJ08782.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07H02; -.
DR STRING; 316055.RPE_4863; -.
DR KEGG; rpe:RPE_4863; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABJ08782.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ABJ08782.1}.
FT DOMAIN 113..166
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 349..573
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 597..710
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 299..340
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 648
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 723 AA; 78302 MW; C8095860CE618238 CRC64;
MPSADIPDFL RGGGEMGARI AAFDWASTSL GPIALWPPSL KTAVALVVHS AVPLVMLWGE
DGVMIYNDAY SVFAGRRHPK LLGSKVREGW PEVADFNDNV MKAGLSGRTL AYRDQKLTLY
RHGAPEPVWM NLDYSPVLDE SGRPAGVIAI VVETTKRVRA DQRIAAEQDR LLSLFDQAPG
FMAMLDGPEL VFTLANPAYL RLIGHRPAMG RRLRDVLPEL RGQGFYEILE HCYRSGEPFV
GNSLKVSLQP VQGGPFEDRF VDFVFQPVRD GAGAVTGIFV QGSEVTERVE SEVALRRLTE
TLEARVEERT AELAAANRQL VNQIEERERV EATLRQMQRL EAVGQLTSGV AHDFNNLLTV
VLGNLGFIDK ALVAAGVDDK SRNRLANIRA AAERGATLTA QLLAFSRKQR LEARAVDLNE
TLAKMQELLR SSMGGSVRLE LVLQPELWPA LVDPTQIELV ILNLAINARD AMQVGGSLTV
ETANVRLAAP SRPEMPAAGE YVMIAVSDTG TGMTPEVLAK AFEPFFTTKP VGKGSGLGLA
QVFGFAKQSG GGVRIDSQFG EGTTVKVFLP RGTGHLAVAD QAGPPEDTLE LSGAARRVLL
VDDDSAVRDV AASMLREQGC VVVEAGSGGA ALDLLERDPV PFDLMVIDFA MPGMTGAEVA
REVKLRRPGL PMIFITGYAD LAAVKNLGAD AIVQKPFRDD ELLHRVRRLL GTPRSGNVVP
IRK
//
