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Database: UniProt
Entry: A0A1U9LHE3_9PROT
LinkDB: A0A1U9LHE3_9PROT
Original site: A0A1U9LHE3_9PROT 
ID   A0A1U9LHE3_9PROT        Unreviewed;       832 AA.
AC   A0A1U9LHE3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A0U91_01740 {ECO:0000313|EMBL:AQT05884.1};
OS   Acetobacter persici.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1076596 {ECO:0000313|EMBL:AQT05884.1, ECO:0000313|Proteomes:UP000189055};
RN   [1] {ECO:0000313|EMBL:AQT05884.1, ECO:0000313|Proteomes:UP000189055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMW2.1084 {ECO:0000313|EMBL:AQT05884.1,
RC   ECO:0000313|Proteomes:UP000189055};
RA   Brandt J., Jakob F., Vogel R.F.;
RT   "Acetic acid bacteria sequencing.";
RL   Submitted (MAR-2016) 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; CP014687; AQT05884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9LHE3; -.
DR   STRING; 1076596.A0U91_01740; -.
DR   KEGG; aper:A0U91_01740; -.
DR   Proteomes; UP000189055; Chromosome.
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   Gene3D; 3.30.450.270; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; 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:SF8; 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          127..286
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          720..831
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         770
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   832 AA;  92964 MW;  66AF3F1D1BAACDCC CRC64;
     MHIPGSIQPH GCLLACEREG FRVRRLSANA ASMLGLEGLA PGSLLSDHLS AATLHTLRNA
     LANSLSLGRP AYVFGEQITQ HARFDLSVHM SGEDMVIECE PEGAPEDNNQ FVSNLRMMLD
     RLRDIADMER LFSAVVRLMR GMLHYDRVMI YRFDPDWSGK IVAEARSSAL ESFLGQHFPS
     ADIPVQAREL YRRALIRMIG DVSYTPVPMQ QLPGLGALDM SLSQLRSVSP VHCEYLSNMG
     VGASMSISLM VDGKLWGMIA CHNYSPKILT LGERTIVKIF GEFVALRIVV LLRTSRLHVT
     QQTHSLIENF LRDAVPMSDM PSYLREHIAD LAPLIPCDGI GLWIDGQWTT YGTAPSAPET
     VLSLVSIAHE RAGHQIWHTD HLTDIVPDAP AMLPDVAGVM IIPISAQPND YVFLFRPEIL
     QTLNWGGDPN KTYTNGPLGP RLTPRTSFAI WKEEVREKCL PWTDNNLEAA GLVRSGLIEV
     MSAYHQQQLK ERAQADTRQR MLNEELSHRV KNILAVVRSL MAQPVPEGRT LQEHFDVLQG
     RVKALAHAHD QVVRTDGGGL LYPLLDAELA PYRLLPDTIT LSGPPVWLTG RALSVMALIV
     HELATNAAKY GAFSTQEGRL HVRWWQDEAT QDWVVTWQET GGPTISRSTR KGFGSILLDR
     AVPHELHGKT QKEFRTEGLF IRFDLPAHHA ELITQENSTM QEPVRADVMQ ADRIRLQDKN
     ILIVEDQLLI AMDVEQALAD YGLSQVRSVS SVYEALQAIR TDQPDCALLD FNLGDETSAD
     IARALREREI PFLFATGYAD RSMIPTEFRD VPVVRKPYAP ATLIREMEKL LS
//
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