ID Q07VE3_RHOP5 Unreviewed; 1060 AA.
AC Q07VE3;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RPE_0130 {ECO:0000313|EMBL:ABJ04091.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ04091.1};
RN [1] {ECO:0000313|EMBL:ABJ04091.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ04091.1};
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; ABJ04091.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07VE3; -.
DR STRING; 316055.RPE_0130; -.
DR KEGG; rpe:RPE_0130; -.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_12_5; -.
DR OrthoDB; 9796100at2; -.
DR GO; GO:0005886; C:plasma 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 DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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 NCBIfam; TIGR00229; sensory_box; 1.
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; 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; 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 SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABJ04091.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABJ04091.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 346..397
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 409..445
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 487..540
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 541..592
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 619..669
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 682..905
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 927..1043
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 905..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 977
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1060 AA; 115428 MW; AEA9FF716CC1B282 CRC64;
MKLSTRMALA MVALVLVTTG VLALLTYYNV ISLVLPRALD RLQVHSRVAA TMLDASVQGI
RADALSAQAS PALRSLGPTR VEGLDPDHRE TGADLRARIE NRFVADLAAK PEYALIRIIG
TADGGMELVR VDRLGPDGAI RIVPTSGLTR RGDRAYFKEG VQLPPNYVHI SKVELNKNDK
GLEVPHAPTI RASAPLYGSD GKAFAVLVIN FNLGPALERV RASLTGGREA FVINEAGDYL
VHPADPSKEF GFDLGERHRI QDDFPDFEPM LKADRSEPRV MTRRDGARYG LGWEWVRLAG
GPRVAVVEVR SYGVLTSVGS AVSNSTLIGG GAAMLCAILM AIAMARSLSR PLVQITRAVE
GFGRGELIRV KPGGGTEIAA LAQTFLNMTA EAQRKSAALS DEIAARTHVA EMLNNTLTNM
ADPVVIADAG GSVVLTNVAA AKLFGQPIDI GNPQAYRSFE RFCPDGVTPL PFEQSPLLRA
FRGEVVENFE FSARPLGSDR MSYLVANGRP LRNEAGKLQG AVMVYHDITQ TKTAEHELRE
SERMAHAIID TALDAFVQID RTGAITEWSP HAETMFGWPR NEALGRHMAD LIFCSEQIGE
LAVRYRNFIE SIERGGSGYR IEIEAVRRNG TPIQVEVSMT ALSRNDGYVL NAFFRDLTDK
TIAEQQLRQA QKMESIGQLT GGIAHDFNNM LTVITGTIDI LAASVADRPE CAAITRLISE
AADRGAELTR HLLAFARKQP LEPCETDPNV VLSELQILLR PTLGEHIEIR ESLQDGVWPI
FVDRGQLEAA LVNLAVNARD AMPEGGTLTL ETRNTMIDQD FVRRYGEGEP GQYVMITVTD
TGCGIAEAIR VRVFDPFFTT KEVGKGTGLG LSMVYGFIKQ SGGHITLYSE VGHGTAFRIY
LPRAKSEARQ PDSDPEPSGT ELGGSETILV VEDDTMVRNY VIAQLKALGY HTVAAANAAA
ALELCSQGVA FDLLFTDIVM PGKMNGVQLA IAMAKRRDFL KVLYTSGYSE NAVIHNNRLD
PNILLLTKPY RRSELARMIR LALTSEPFQP EHIPAAASSP
//
