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Database: UniProt
Entry: A0A368W3I2_9BACL
LinkDB: A0A368W3I2_9BACL
Original site: A0A368W3I2_9BACL 
ID   A0A368W3I2_9BACL        Unreviewed;       602 AA.
AC   A0A368W3I2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-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=DFP97_104137 {ECO:0000313|EMBL:RCW49479.1};
OS   Paenibacillus prosopidis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW49479.1, ECO:0000313|Proteomes:UP000252415};
RN   [1] {ECO:0000313|EMBL:RCW49479.1, ECO:0000313|Proteomes:UP000252415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW49479.1,
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RCW49479.1}.
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DR   EMBL; QPJD01000004; RCW49479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368W3I2; -.
DR   OrthoDB; 9759607at2; -.
DR   Proteomes; UP000252415; Unassembled WGS sequence.
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   CDD; cd00082; HisKA; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd18774; PDC2_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR033479; dCache_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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; SSF103190; Sensory 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000252415};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        283..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          306..362
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          384..598
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          350..377
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   602 AA;  69127 MW;  4C7236D2E23CE1C0 CRC64;
     MNLLLRVFRL QSLKARLRFL GIALVLMVGL STISSYSFLQ YRQTENNQIN SMRKDGAIQQ
     TAIDNWVATR ASEIRNLANM QSTIELNIDE IENNLIFFAS HQQEFEAVSF ANKEGIVEFS
     TMNQIGAYFT ERTYWEEAAK GREYISDVLM GKVTNQPTIL FSAPVMNKNK QFLGVIYGTV
     SLKTIDQFME QFQSGDSGES YLIDRNGYLI TESRFAGNWK ILEYKLNSDI LERAKQGVQS
     ASTYENYRGK QVFGTYQLVN NGKWIAVNEI ERNEVYRTFN QQLIVMIIII GIVLIFGIIV
     TLRISYLIEH PVQHLLKGVQ RLRKGDYQYK IDYSGMKSAP VELLQLCEAF NQMSQNIQDN
     ELELKRQKEE LASSNAELEQ FAYVASHDLQ EPLRMVASYV QLLAKRYQGK LDQDADDFIH
     YAVDGSQRMQ NLINDLLIFS RVGTKGKELK SVDFEVVLHH VMANLQHAIQ ESDARVTHDP
     LPTLMADSTQ MVQLLQNLIG NAIKFRDANR APIIHIGIKQ QDRDWLFSVQ DNGIGFDPRY
     RDRIFLIFQR LHNKTKYEGT GIGLSICKKI VERHGGKIWV ESEAGHSTTF YFTLPDRGEH
     IT
//
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