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Database: UniProt
Entry: W4C5S2_9BACL
LinkDB: W4C5S2_9BACL
Original site: W4C5S2_9BACL 
ID   W4C5S2_9BACL            Unreviewed;       621 AA.
AC   W4C5S2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C162_11531 {ECO:0000313|EMBL:ETT50887.1};
OS   Paenibacillus sp. FSL R7-269.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1226755 {ECO:0000313|EMBL:ETT50887.1, ECO:0000313|Proteomes:UP000019056};
RN   [1] {ECO:0000313|EMBL:ETT50887.1, ECO:0000313|Proteomes:UP000019056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-269 {ECO:0000313|EMBL:ETT50887.1,
RC   ECO:0000313|Proteomes:UP000019056};
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:ETT50887.1}.
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DR   EMBL; ASPS01000021; ETT50887.1; -; Genomic_DNA.
DR   RefSeq; WP_036694466.1; NZ_ASPS01000021.1.
DR   AlphaFoldDB; W4C5S2; -.
DR   PATRIC; fig|1226755.4.peg.2308; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000019056; 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; cd12912; PDC2_MCP_like; 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; 2.
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; 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; PF02743; dCache_1; 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, ECO:0000313|EMBL:ETT50887.1};
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        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          332..384
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          426..614
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   621 AA;  69481 MW;  26226523A261B106 CRC64;
     MRKTGVTMEK LKLNNMPIRY KLIIHFLLIS ILPSIGLGLL IGWTVDRIVE EQSTENTMQL
     IRKVNTAIES DVENLQKITY LISFDPGVQK FLKGEPPVPA QPDPAAGNGE SAEYNIRKFL
     QGFTTLSSEI AGIMLVNREG GFISNEMYTR SGTRLTEESW YKQAVENKGI FLIVGHPYGR
     AVRSHVDYKE SEVVSAVRAI VNPETQVVQG VVLVDLKLRV IAETARDVTL GKTGYLTVVD
     NRGEMIYAPQ HPLMRTIPAG LFTESSGITS ETVDGRKLQL IYRTSPFTGW TTMGVFPMDE
     SAYGIREITF NVVTFVFVVC MLGMTASFYL AYSISRPIGQ LASFMSKAQS GDLTIRYWGS
     RSDEIGLLGR SFNTMLAQIG RLLSLTELQA RQKREAELRS LQAHIKPHFL YNTLDTIHWM
     ARSKGAEDIA EVVQSLSRLF RLGLSKGSDI IPLSDELEHI VSYLKIQHVR YSTKLTYSIE
     VEPHLQELYV LKLLLQPMVE NAIYHGIKER RGPGLLSIAV VERDNDLYLT VRDDGAGMSA
     DKLRELRRRL EAVGTEELER TETDMAGTGS AGSGYGILNV QARIRLTYGE PYGIQIESGP
     GQGTLVTVRH PVVRESYPEK Y
//
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