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Database: UniProt
Entry: A0A089K729_9BACL
LinkDB: A0A089K729_9BACL
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ID   A0A089K729_9BACL        Unreviewed;       636 AA.
AC   A0A089K729;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=R50912_23750 {ECO:0000313|EMBL:AIQ42728.1};
OS   Paenibacillus sp. FSL R5-0912.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536771 {ECO:0000313|EMBL:AIQ42728.1, ECO:0000313|Proteomes:UP000029512};
RN   [1] {ECO:0000313|EMBL:AIQ42728.1, ECO:0000313|Proteomes:UP000029512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R5-0912 {ECO:0000313|EMBL:AIQ42728.1,
RC   ECO:0000313|Proteomes:UP000029512};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP009282; AIQ42728.1; -; Genomic_DNA.
DR   RefSeq; WP_042238130.1; NZ_CP009282.1.
DR   AlphaFoldDB; A0A089K729; -.
DR   KEGG; paeq:R50912_23750; -.
DR   HOGENOM; CLU_020473_6_0_9; -.
DR   Proteomes; UP000029512; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029512};
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        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          341..393
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          376..627
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   636 AA;  72420 MW;  91C79AD5735C5691 CRC64;
     MARVRSTAEK LKRWLADLSI QIKLIGAYIV IILVPVIVIS NYLFTGFYQN TIKDIIKENR
     YQTDNEKQEI MSRIGVMEQS IGLLVSDRQL REYVTVESEP GLNDIKRFQE YSFTYLQTVL
     FNNSDIANIH FFVNNPWISE LWPIIYHEER IKDKPFYTKM LNQTGNVLWE IQSEDAILQD
     SNAAVNQSLS SIVSLMAGVN QMNSQNLFQH LGIVKVDMPI GNFFKKAYNN SSDRDSRFYI
     LDQQGNLHAN STDPLAGLDE ADIQPAVAKY KEAGKSSLLL SHKGEDFLYL VEHIDKINAE
     LINVISLHTT YSKIDQTRNT VIVVIIILLI LLAITTFFMQ SIILNKLNIL RDSMKQVRGG
     DFGVDIDVKG GDEIGELAHH FRQMLNTING MIADAVKRSA ATKEAELQAL HNQIDAHFLY
     NTLENLKMLA EVEGQYTVSD ALTSLGSMMR YNLRWTGDRV QLRDEMGHIQ HYIAIMSIRY
     DEKLKLEIEV EDEFWDHEIL KMSLQPIVEN ALKHGVYSAL MKSDGLIVAI HAFEDGGFFY
     IEVTDNGIGI AEDKLQELNR KQIMSEEEFN ALPREKAETT ELNKGSGIGL RNVNQRIQMV
     YGNEHGLRIE SKRGSYTQVT VKLPLIISSR GGTQII
//
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