ID A0A368VSH1_9BACL Unreviewed; 584 AA.
AC A0A368VSH1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DFP97_11389 {ECO:0000313|EMBL:RCW43417.1};
OS Paenibacillus prosopidis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW43417.1, ECO:0000313|Proteomes:UP000252415};
RN [1] {ECO:0000313|EMBL:RCW43417.1, ECO:0000313|Proteomes:UP000252415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW43417.1,
RC ECO:0000313|Proteomes:UP000252415};
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 (JUL-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:RCW43417.1}.
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DR EMBL; QPJD01000013; RCW43417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368VSH1; -.
DR Proteomes; UP000252415; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR032834; NatK_C.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR PANTHER; PTHR40448; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR40448:SF1; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF14501; HATPase_c_5; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RCW43417.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000252415};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 480..584
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 584 AA; 66792 MW; 63AD372AC477FFD0 CRC64;
MREMQRNIWL MAISVIVVLI LLNNTAYYFL TKKTLNDSFN EELLAHAKRL EISLEQSRQG
AEQFQDQIGR ELRAASIAAQ YALDPDIEKV TNEQLKELSD KLGISHITLL KKLPDDIVLY
KSSDETQLGK STKTWKPWYE VFNQLFDRHN VSVDWLGQTL PNFWSGPFEV SSTDLDKVNK
WGYYYDGATN YIIDPYVGYD RQEEYEDATG VHRMIENSMQ TSESLLEIAF INPETFPDGK
QTVHPNGDVQ DHKVQQPIFY GKYTIKSEKD TALVRKAYLT KEIVTLNEKI DGKEIYKMFI
PVFATDKGIN ITDEDGIPLD SYVLSLTSDY HIIQEQLDSQ FLNLGVIIII LTCLSLLIAV
IAMRYYKQSR DKAVRVTQET YVEEINQMFQ SIRAQRHDFL NHVQTIHSLA ELEKSKELVA
YTKELTGDIR LMNDIINIGN PAIAALVRSK ISQAENYKIQ FSCSFSGLNM QEMGVKTLDV
NRMLGNLIDN AFDEVLKFPE ERRHVTLIGR QTAHELEFTI SNTCEQAEEA VVKPLFDAGF
STKQQDHQGL GLSIVKSIAE QYKGNVYVTA EPNGQLTFIV KIPI
//