ID A0A2V5KMW5_9BACL Unreviewed; 858 AA.
AC A0A2V5KMW5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DLM86_06430 {ECO:0000313|EMBL:PYI56600.1};
OS Paenibacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI56600.1, ECO:0000313|Proteomes:UP000247476};
RN [1] {ECO:0000313|EMBL:PYI56600.1, ECO:0000313|Proteomes:UP000247476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DXL2 {ECO:0000313|EMBL:PYI56600.1,
RC ECO:0000313|Proteomes:UP000247476};
RA Dai X.;
RT "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL Submitted (MAY-2018) 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:PYI56600.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QJVJ01000002; PYI56600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5KMW5; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000247476; Unassembled WGS sequence.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 4.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 5.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000247476};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 9..78
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 82..134
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 135..207
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 261..321
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 329..384
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 385..454
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 457..509
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 510..581
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 585..637
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 650..855
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 368..395
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 858 AA; 95382 MW; DA08874016EC1996 CRC64;
MSIVEKLRNE ALFREAFWQS PIGVAIMDAD GRLVQSNPAA SSLLGYRDRL PEGPFCRLVH
PDDRAEADAR YRATAGGKCD GDRFEARCVH RDGRAVWMQI DCSLVRDESG TPSFVVVQMQ
DISDRKSADM QLQLNKLWYQ SLFDHHPDLI YAMDLEGYYT AVNRAFEKAI GYTAEQVAAR
GMHFRELTAP EMLERTARHF REAANGLPQR YESVAVDRYG NRIVFDVLNI PIVVEGKVVG
VHGIAKDVSM EKELWDRLER SQRMYRIISD HSQDIISYCD PDGTLLFVSP AYENILGYEP
GEVIGLPATF NWHPDDVAAL RANGVLRHSD AETFVSRVRH KDGRDVWIET TATIIRGKDG
GVESIMGVGR DISERKRAEE ELRRTKERLE SFVRNNADAI WVIDAEGIVL DTNEAFATLF
QWKTQEIVGK PLPIVPPYLK PYIDSLHEKA MGGTSVSGLE TVRLRKDGST VEVSMTLSPL
RDSAGAVVGL TGICRDISER KRAENELKAA IERMQSFISH NVDPIMIFDA GGKLVQVNES
FERLFGWSSG EIAGLGPRDF AFVPDDREAE SDQTAELLRT GKPISGFETY RMCKDGSSVS
VSVTAFPLRD GEGRISGCCV TLRDTTERKQ AEELLINSEK QSIAGQLAAG IAHEIRNPIT
AIKGFIQLMN SGFPGKREYF DIIASEIGRI ELILNELLVL AKPQTVKYER RDVGKLLTQV
IALLESQAIM KDVQLAADFE CGDVFVWCDE NQLKQVCINF IQNAIEAMPD GGEVVVRLAR
AGEGRIAVAV VDRGCGIPAH LLSKLGQPFY TTKEKGTGLG FMVSKRIIES HAGDLTVESR
EGAGTTVRFT LPIADEMP
//
