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Database: UniProt
Entry: H6CKM8_9BACL
LinkDB: H6CKM8_9BACL
Original site: H6CKM8_9BACL 
ID   H6CKM8_9BACL            Unreviewed;       614 AA.
AC   H6CKM8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=WG8_3421 {ECO:0000313|EMBL:EHS57151.1};
OS   Paenibacillus sp. Aloe-11.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS57151.1, ECO:0000313|Proteomes:UP000005078};
RN   [1] {ECO:0000313|Proteomes:UP000005078}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aloe-11 {ECO:0000313|Proteomes:UP000005078};
RX   PubMed=22461553; DOI=10.1128/jb.00087-12;
RA   Li N.Z., Xia T., Xu Y.L., Qiu R.R., Xiang H., He D., Peng Y.Y.;
RT   "Genome Sequence of Paenibacillus sp. Strain Aloe-11, an Endophytic
RT   Bacterium with Broad Antimicrobial Activity and Intestinal Colonization
RT   Ability.";
RL   J. Bacteriol. 194:2117-2118(2012).
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}.
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DR   EMBL; JH601056; EHS57151.1; -; Genomic_DNA.
DR   RefSeq; WP_007431408.1; NZ_JH601056.1.
DR   AlphaFoldDB; H6CKM8; -.
DR   HOGENOM; CLU_020473_6_3_9; -.
DR   Proteomes; UP000005078; 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; 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; 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   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:EHS57151.1};
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|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          341..393
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          503..607
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   614 AA;  71400 MW;  B325436785D0E72E CRC64;
     MKRGNRYTAY FKNNMFLRIL LLFSCIVILS IITIAYVTYI SISQSMIRRE LDTQKAAMES
     VDRYIHLRHE SVQNMVRDMY RNEALSMNVS FFMDHAYSEY VQHRMDETYM ESHDYSTDVL
     TYFKNWLDEN SDISNLILYS ADQQYLSTFN ENKQFKQFPV HAARSFVPDV MAAESKSVSA
     PNYWIRKAVD QWSPSLYSLQ VPINNKQTLK NTGQLLVFLN SKSISNALTS YGNNLKGEII
     VLSTHGTVLF DSRNNYYGKT YPYVEVTRSL YDDVDSDVGI IQAKQNMYIN KLISPDEGYV
     VIGAVPNEEM AESYRGIRNT ILTISVVCIL FAVLFPAFFV INFAKRTNRI IKFTRQVKNG
     DLTARIQDPQ EDELGQISRS FNDMLDELNL YIERVYKAEI KQKQTELVAL QARIHPHFLY
     NTLEVIRMRA ISQGAKDVGE MIYSLSVLFK SLVQQKKIYT LKDELEACRL YLELFRIRYK
     ERFNYTITVD PELYTRSVMK LMLQPIIENY IVHGIQSDRN DNVLTIDVRE TGEILLVEIR
     DNGKGIEGER LKQILEELER QEENGQMFGL RSVHTRLRFL HGADYGIELE SRSGEGTTIR
     VRCPNREGMD AIYV
//
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