ID Q01WP9_SOLUE Unreviewed; 1210 AA.
AC Q01WP9;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Acid_4959 {ECO:0000313|EMBL:ABJ85916.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ85916.1};
RN [1] {ECO:0000313|EMBL:ABJ85916.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ85916.1};
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 Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-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; CP000473; ABJ85916.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01WP9; -.
DR STRING; 234267.Acid_4959; -.
DR KEGG; sus:Acid_4959; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_0; -.
DR InParanoid; Q01WP9; -.
DR OrthoDB; 111890at2; -.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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; 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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABJ85916.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 222..272
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 273..344
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 346..398
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 473..525
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 709..780
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 782..834
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 847..1070
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1091..1208
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1142
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1210 AA; 134014 MW; D563267F33239592 CRC64;
MEPPLDDLAF DDLTALAAGI CEAPMAVLSF VDEDQEWFQS NVGVATGPIA RNVSFGAHTI
LQPDLLIVPD AGEDARFAKN PLVTGDPHVR FYAGVPVLNE GGAAVGALSI MGRDPRQLSL
AQQHGLRALS RQVTALMELR RHRLELTEGE AQLFRVLRGC PIALTVHRMS DGAFVDANDI
FTSLTGWSCK EVIGHKAPEL QLVDGATAAR LRSQLEACGE LHNAETTVRT RSGELRKVLL
STALVELRSG LHAITTFVDI TERKRAEDEL REHKRRLAAI IEHEPECVTV MDAEGRLLEM
NPAGLAMLDV ESLAEAQEKP LVDYVSPEYR AVFQRLQKKV LSGGSGTLEF ELVGRRGTHR
WLETHAAPLR DAAGHVEALL SVTVDMTRHK AAEEELREKH GQLQSALELA RAGVWHWNSR
TDRVRTIQGS GPVSGLPKSS YPSNRAAFLL LVHPDDRADI AGKLERARST GEFAAEFRIV
LPDGSTRWVA ARGRAVRDSS GAAVGLAGVD RDITEQRRAE RRIRQLNRVY SVLSDINETI
VRESNRQRML SEACRIAVES GEFRLAWIGL RSEPGGRIEV AAHAGATEDT VELLHLMSEE
EPGHDECAFT AYAMETGRHG VCNDLARDER AAPWREMALQ RGYRGMASLP LKSGGAVIGI
FNLYAGEPDF FDADELRLLD ELALDISFAL EIYDRETKRG WAEQVLRESE ERFRQLAENI
QEVFWMTADQ KILYVSPAYE RIWGRPRSAL YEDPRSWIEA VHPDDRGQIL QAAKVIQKGG
NYDETYRIQR PDGTVRWIHD HAFPVRDERG EIVRIVGTAE DITERRQLEE QYRQAQKMEA
IGQLAGGVAH DFNNLLTVIH GYGSLLLAGK ESTSGTSLAA QEIVLAAERA ANLTRQLLAF
GRRQVMQPRS LDLTEVVSSL TSMLQRVLGA NIRLQLIPHG SPLITRADSG MLDQVLMNLV
VNACDAMPDG GQLTIETTER TFTQREARRI PDARAGRYVS LRVTDTGSGI SPESLPHIFE
PFFTTKQPGK GTGLGLSTVF GIVKQHGGWV QVKSEVGRGT SFQIFLPAAE ETDEARAAEI
EKPEPQGGSE TILVVEDEPA LRVLTRAVLE PRGYRLLEAA NGVEALRAWQ EHRGSIHLLL
TDIMMPEGMS GLELAARLRE FRPELRVIYT SGYSGDIAGG QLQLEEGRNF LQKPYSPQQL
LEAVRRCLDI
//
