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Database: UniProt
Entry: W4DQJ1_9BACL
LinkDB: W4DQJ1_9BACL
Original site: W4DQJ1_9BACL 
ID   W4DQJ1_9BACL            Unreviewed;       609 AA.
AC   W4DQJ1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C173_16506 {ECO:0000313|EMBL:ETT70294.1};
OS   Paenibacillus sp. FSL R7-277.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT70294.1, ECO:0000313|Proteomes:UP000019051};
RN   [1] {ECO:0000313|EMBL:ETT70294.1, ECO:0000313|Proteomes:UP000019051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT70294.1,
RC   ECO:0000313|Proteomes:UP000019051};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT70294.1}.
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DR   EMBL; ASPX01000054; ETT70294.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4DQJ1; -.
DR   PATRIC; fig|1227352.4.peg.3305; -.
DR   eggNOG; COG2972; Bacteria.
DR   Proteomes; UP000019051; 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   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; 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; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
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, ECO:0000313|EMBL:ETT70294.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        306..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          329..381
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          492..602
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   609 AA;  68488 MW;  FD3D9880F0BE25F6 CRC64;
     MLRGLILRLR RSKMRTRLLL LFTMLTLLPL SVQGMVTYRH FSSTLNEKTK QYTVDVAGQA
     NANLDRLLKD LERLSLMPLY DEQVLSILAK YDGPMGSGTW ALSDDYQKMK LYTSAQAYDR
     PEIRGIHLLS NSGTLFSNVE PLAVNTSWDG RHDEWFSALK RSDGEWILLP PHHPSYYAGT
     DPSSYISVAR VIKEPRTLKR LGYILIDAKQ SAFGSVFSKL KIEESTNLMI IDGEQRLLYE
     QKPDNGQSAY GELMGSGRIK ELHGGERERL GGTDYLFVSH KSPYSGLSVI GLTPIGVMLK
     ESRAMMIFTL WLALFCLVTV LLLAYAVSYR ITLPLVELKS NMSRVERGDF NMRVSPLGGD
     EFGQLGRGFN KMMEEINRLF HEVLVIGLRE KEAELSALQS QINPHFIYNT LESINMMAVQ
     RRHDEVSDMV SALGKLLRYT IDKAGRLVSL GEEIAFVDSY VRIQQIRFGG KLTVHNEIEE
     EVQHLRIPKL TIQPLVENAI DHGIAGREEG TIWVSALRFD NELLITVRDD GNGLEEEELT
     ALNREIEQDP SMDSLRRSEE ESLGLRNIGQ RIKLLYGEGG SLTVDGSPGQ GLAVTITITI
     PESGGEEDV
//
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