ID A0A0Q4LG27_9SPHN Unreviewed; 860 AA.
AC A0A0Q4LG27;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF00_04265 {ECO:0000313|EMBL:KQN31979.1};
OS Sphingomonas sp. Leaf34.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN31979.1, ECO:0000313|Proteomes:UP000051932};
RN [1] {ECO:0000313|EMBL:KQN31979.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN31979.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN31979.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN31979.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KQN31979.1}.
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DR EMBL; LMLC01000001; KQN31979.1; -; Genomic_DNA.
DR RefSeq; WP_055874539.1; NZ_LMLC01000001.1.
DR AlphaFoldDB; A0A0Q4LG27; -.
DR OrthoDB; 9760752at2; -.
DR Proteomes; UP000051932; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 1.
DR InterPro; IPR009219; Bactrphtchr_CheY.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
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 InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF07536; HWE_HK; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF036397; Bactrphtchrm_rec; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 145..302
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 744..855
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 794
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 860 AA; 93675 MW; E6F7D1ABAC50EF5B CRC64;
MSDTIDQSIP DLTICDREPI TRLDRIQSFG FLLALSNDWV IARASANAAD MLGTAADRLI
GQPLDTLVSG QALHDIRNRM SILQATSSER LYDIGLITPK KRFDLSLHFS GDLLILEGEP
SRPQDRIDAA SMVRSMIERL RRTTTVTDFH RDAARQVRAI TGFERVMIYR FDDNGDGDVI
AESTRSNTES FLGLRYPASD IPVQARALYL ANPFRIIPDV QAPTVPVLPV RGQPDQALDM
TYAVTRAVSP VHIEYLTNMG VGASLSISII VEGRLWGLIA CHHSEARCPS FVMRTAAELF
GLMYSMTLES RLRGNTAVDE RNARALSDRM MMAIAGDETL LTNAAWIRDN VGGMIQCDGV
AVFRPGAVTL NGSTPPEGDI ATIARFLDTT SPSRVYDTNA IAVIDPGLAQ SADRAAGMLA
IPVSRTPRDY IMLFRRELLE EVRWSGDPTK AVVKTEDGLR LSPRKSFAAF AEMVRGKASP
FSDADRRIGE AVRIAIIEVI LRYSEAASGE RRRSTERSTL LIAELNHRVR NILTLVRGLI
ARTGQSATSV AEYTTALNGR VQALARAHDY VTRNSWGPAS LVALLEDEVN AHRRNAHDVL
LIDGPLVHLQ PTAIATMALV IHELATNSAK YGALSTEGVV HVALDLRADG GLDIRWRELG
GPPVQAPTRR GFGSVVIERT VPFDLQGTAE IRYSLSGVEA DFFIPAKYVV ASSGDAEIWF
EPAAPDEPHV DSGSPETSPI TGTSILLLED SMIIALETED MLYALGAGKV TTASTIAEAH
ALVSANHFDL AVLDINVAGQ VSFDFAHRLK TDGVPYVFAS GYGDQVVLAG EEAGTIVLQK
PFEIDHLRQA LLMCIETRSA
//
