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Database: UniProt
Entry: A0A089ITR7_9BACL
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ID   A0A089ITR7_9BACL        Unreviewed;       595 AA.
AC   A0A089ITR7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:AIQ26655.1};
GN   ORFNames=H70737_29710 {ECO:0000313|EMBL:AIQ26655.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ26655.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ26655.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ26655.1,
RC   ECO:0000313|Proteomes:UP000029519};
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.
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DR   EMBL; CP009279; AIQ26655.1; -; Genomic_DNA.
DR   RefSeq; WP_042192901.1; NZ_CP009279.1.
DR   AlphaFoldDB; A0A089ITR7; -.
DR   KEGG; paej:H70737_29710; -.
DR   eggNOG; COG2197; Bacteria.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_15_9; -.
DR   Proteomes; UP000029519; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd17535; REC_NarL-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR039420; WalR-like.
DR   PANTHER; PTHR43214:SF24; TRANSCRIPTIONAL REGULATORY PROTEIN NARL-RELATED; 1.
DR   PANTHER; PTHR43214; TWO-COMPONENT RESPONSE REGULATOR; 1.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AIQ26655.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029519};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          195..376
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          384..500
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          529..594
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50043"
FT   MOD_RES         435
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   595 AA;  67905 MW;  787B0B0EDF7238D5 CRC64;
     MFNLVKQWFW YDWLVLLFRI CFSTSFIVTM CYLSEDFTIP FWIVFVWGVI SFSVPWFCLQ
     LHYKYYLMAE ILLSGGLCLY LAALFPDSYV TFLPIAFMIA SNSAQKSYRW SAPITVILIP
     IMLSKLSQQM DAISMIVNFG LVYTIGFAFH LLVVNHKQNG IIKNQNAVLE QYISQVERMT
     LLEERDRLSK DLHDTVGHSY TSILMGLETL RTEVNTSEGE QKIDSLLKLT RNGLDDVRKY
     LHHVGSSQDS LTLMQSLQKL VDDFQTFSKV QVRLRTFGEA YTISKQAKMT LYRCLQESIT
     NAVRHGQASE IVITLHYEEK LIRLEVQDNG LGTEDLKAGF GVNAMKERAS NLQGQVYLYS
     KPGEGTLVTC SLPRLEEIQE EMIRLLLVDD QPYIRDSLRI ILEQQPDFEI IGLAENGEQA
     VGFCEQEQPH VVLMDLNMPD MDGAEATKLI KQKWPGVRVL ILTTFQETDL AVEALQNGAD
     GYLLKSTEPQ ELFEGIRLVH RGVKMITPAI TNVLIDHYEM HPTSEAQTEQ SNEYGLTPRE
     LEILECLSKG MRYKSIAAKL YLSDGTVRNY ASTIYAKLGV RNREEAVEKA FGTLE
//
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