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Database: UniProt
Entry: A0A3G9JNW1_9BACL
LinkDB: A0A3G9JNW1_9BACL
Original site: A0A3G9JNW1_9BACL 
ID   A0A3G9JNW1_9BACL        Unreviewed;      1036 AA.
AC   A0A3G9JNW1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Back11_58890 {ECO:0000313|EMBL:BBH24544.1}, FHS14_004432
GN   {ECO:0000313|EMBL:MBB3071423.1};
OS   Paenibacillus baekrokdamisoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1712516 {ECO:0000313|EMBL:BBH24544.1, ECO:0000313|Proteomes:UP000275368};
RN   [1] {ECO:0000313|EMBL:BBH24544.1, ECO:0000313|Proteomes:UP000275368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 33723 {ECO:0000313|EMBL:BBH24544.1,
RC   ECO:0000313|Proteomes:UP000275368};
RA   Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA   Lee J.S.;
RT   "Complete genome sequence of Paenibacillus baekrokdamisoli strain KCTC
RT   33723.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB3071423.1, ECO:0000313|Proteomes:UP000562277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8890 {ECO:0000313|EMBL:MBB3071423.1,
RC   ECO:0000313|Proteomes:UP000562277};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (AUG-2020) 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; AP019308; BBH24544.1; -; Genomic_DNA.
DR   EMBL; JACHXC010000010; MBB3071423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G9JNW1; -.
DR   KEGG; pbk:Back11_58890; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000275368; Chromosome.
DR   Proteomes; UP000562277; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR008979; Galactose-bd-like_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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF02518; HATPase_c; 2.
DR   Pfam; PF06580; His_kinase; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 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:MBB3071423.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000275368};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        393..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          443..660
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          700..817
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          927..1026
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   MOD_RES         750
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1036 AA;  115268 MW;  35CFA40AEC3013F9 CRC64;
     MTRNKAVIAL MILGVMLFLS ITYWHVTSRS VEGRPEAVNG ELDLTQRDFA ADGIVPLDGE
     WEFYSGRLLT PADFDLDKQD GNRPEMTRYV HVPDNWEHYV DKQSKSSPYG YGTFRLRVKL
     PEEAGRIYGI RQTNIKTAHK LFVNGREIGA RGIPEKNKSE TVSVNAPYVR YFSADGNRAD
     IIIQVANYRY FQGGITSSVV LGYQQDIQSA RETAIAKDLL TTSAFLIMGI FFIMLFWMRG
     LERSWLYFGL FSVSFCLYTV THGEKIMSLL LPNIPYELFA KLQDLSGACT QLFLLLYARH
     SFPILFNKPV MRVFGIIAAG QMLFILATPA VVFSHMSVFS FGLAFIGNLY VVYIMSVGAM
     REKDVPFYML IGALSLLFFA AAASLEFIGI GQFSYVALAA WMCFAFTQGL LLSKRFVYAF
     GEVHMLSDRL RSMDRLKDEF LANTSHEMRT PLHGIINIAQ SLLEGAAGRM SSKQEENMAM
     IVSTGKRMSN LVGDLLDFAK LKNGELVLKR QPVALKQVVS VVFEMFRHLA GVKPVRYIEI
     LSDRHVAYAD EDRLMQILNN LIGNALKFTA EGEIRVAARE ENGWLVISVS DTGIGIPQDK
     LEAVFESFEQ VQGSIERGYG GTGLGLSIAR RLVELHGGII WAESELGKGA VFTFTLPLAS
     EAVQKPAATG EKMSLALLET AASAASSSET IRLDGDGTVT VLVVDDDATN RQVLLNLLSL
     ENYTVIAVSS GMEAMHQLEH NRRIDLAVVD LMMPGMSGYE ICRTIRKRYS LSELPVLLLT
     ARSRPEEMLA AFDAGVNDFL SKPVDAGEMK ARIRTLLKMK MSVSESIIAE MAFLQAQIKP
     HFLYNALNTI SAFSLDDAQA ARDLLAKLSQ YLRGSFDFRN MDRLVPLRKE MELVEAYLSI
     EKARFGERLR VIYDVNGDMN CLLPPLVIQP LVENAVHHGL AHRKQGGTIT ISVHTVQDEV
     MITVEDDGAG LTPPMKDQPF GDREAASGVA LRNIKQRLNR MYGRGFTMES KASGGTIVAI
     RIPRGELADD QYNGGR
//
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