ID Q137Y0_RHOPS Unreviewed; 759 AA.
AC Q137Y0;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RPD_2377 {ECO:0000313|EMBL:ABE39609.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE39609.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE39609.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE39609.1,
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., 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., Lykidis A., Oda Y., Harwood C.S.,
RA 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; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP000283; ABE39609.1; -; Genomic_DNA.
DR AlphaFoldDB; Q137Y0; -.
DR STRING; 316057.RPD_2377; -.
DR KEGG; rpd:RPD_2377; -.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_50_1_5; -.
DR BioCyc; RPAL316057:RPD_RS11920-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:ABE39609.1};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Nucleotide-binding {ECO:0000313|EMBL:ABE39609.1};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606}.
FT DOMAIN 154..313
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 541..755
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 759 AA; 83362 MW; DE006AEB0044A8EA CRC64;
MDPVKADGVV TAKNVDLSTC DRELVQYPEA IQPHGAMLTV DDQSHLIMHA SANCAEFLGK
PLEAVVGSTV AAVLGPAWRD LTATLHRMPL DSGPVNIARE SFVGTERGFN LFAHRCGGLI
ILELEKSAAD GSGVSPNLYS EVRADLARLQ DANSLKDFFD LAVARIRAFT GYDRVMAYRF
DVDGSGHVIA EAKRGDLEAY LGLHYPATDI PAPARRLFSL SWVRHLPDVD YTPVPLIAAK
NLLVPGPVDM SVASLRSVSV MYTGYLKNMD VRSTLVMPLV KEGKLWGLIS AMHHAAPRHI
THETRMAAEF LAHTLSLLMS AKEDAELFGL ITAMKATSDR LIRALAVDAN VARALRAPDA
LQLLSTQVEA GGVAIISDQN VTLSGKTPSR DEVRDLAGWL TDRTSPLFAT DRLPSLYAPG
EAFARDASGV LAVRISPKLP DLVLWFRPEQ VEIVAWAGDP HKPVDVSEAD GMLRLRPRNS
FALWKESVRN RSIPWRDDEK EAVARLAAAI GDIVAERATR VERISRELGG ARSELGHYAD
TASHELKEHL RGIHHLTTAL RRRHGDVLDD EGQQQVVTIL KLTQRMESLV DALLEQAQTS
RSELALQTAD LDAVVDAAML PFARQFAEEN IEIRRPGPLG TATCNKEWVG EVFSNLIGNA
IKYNDKPARW IEIGVEQGHP ARYYVRDNGI GIEETDQQLI FQMFHRLNEP EQYGGGAGVG
LAMTRKIIER HGGRIWVRSR PGDGSTFYFT LSPDDGNGI
//
