ID A0A2A3UAR6_9SPHI Unreviewed; 756 AA.
AC A0A2A3UAR6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CNR22_12600 {ECO:0000313|EMBL:PBQ32575.1};
OS Sphingobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=2021370 {ECO:0000313|EMBL:PBQ32575.1, ECO:0000313|Proteomes:UP000217505};
RN [1] {ECO:0000313|EMBL:PBQ32575.1, ECO:0000313|Proteomes:UP000217505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-48 {ECO:0000313|EMBL:PBQ32575.1,
RC ECO:0000313|Proteomes:UP000217505};
RA Choi A.;
RT "Draft genome sequence of sphingobacterial strain SH-48, isolated from
RT freshwater in Korea.";
RL Submitted (SEP-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PBQ32575.1}.
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DR EMBL; NVQB01000001; PBQ32575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3UAR6; -.
DR OrthoDB; 9766459at2; -.
DR Proteomes; UP000217505; Unassembled WGS sequence.
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 Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PBQ32575.1};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000217505};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000313|EMBL:PBQ32575.1}.
FT DOMAIN 147..304
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 531..756
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 504..531
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 756 AA; 86201 MW; 4C9A805C2C893BC9 CRC64;
MKIKDIVNRD LVNLQNCESE PIHIPGSIQP HGFLLAVKQS NYQIDFCTAN SFDFTGIKHT
DLLGKSFEEV FGDDEGKKLK DYVADPLSDA SKPHVFNWNG IPYNTLIHKS GENFILDLEP
FPDGSLTLPD LYSQTKRFVS HLERSVTLQD LCKIIAEETR SITGYDRVMV YRFDKEYNGE
VFAESKRDDL ESFFGLHYPH TDIPVQAREL YMRNLMRIIV DVNYTPVPIF TIDDVKDKNL
DLSNSVLRSV SPIHIEYLHN IGVGATLTIS LMHNKKLWGL IACHHYSPKN LPHYTRLAAQ
LQGHFLTSQI NVREVAEEFD LSQSIANSLE NLMRNIPEVS SGNFHHVMNE DLLKITNSSG
AVLISEGMLR SFGQIPAEKE ISSLVKWIAA KHETGVYITS KLIEEYPRAE KIRECASGVL
FHALGNPIND SIIWFRQEVQ KTVNWAGDPN KAIIKNEKGL SPRKSFELWK ERTKHQSEEW
EEPELVAASK FAHALQKQTY VLYLTREETK YRELSEKLQK ANSELENINW ISNHDLKEPL
RKIQVFASKI LEDDNHNLSE FAMGSVQKMN DAASRMQTLL NDLMSYSQLR DTSDAFSKVD
LNGLLKNVQD ELKEELQEIT AEVEFSDLPE VNGISFQLHQ LFLNLIRNSL KFSKADIRPH
IKITSTQEQV ESDIQGLEMG RTYYKVSFSD NGIGFNNDHS QTIFNVFKRL HSAKKYTGTG
IGLAICKKIM ENHSGHITAE GEVNVGSVFN LYFPVV
//
