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Database: UniProt
Entry: A0A0K9GTG3_9BACI
LinkDB: A0A0K9GTG3_9BACI
Original site: A0A0K9GTG3_9BACI 
ID   A0A0K9GTG3_9BACI        Unreviewed;       483 AA.
AC   A0A0K9GTG3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AC625_10750 {ECO:0000313|EMBL:KMY49940.1};
OS   Peribacillus loiseleuriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY49940.1, ECO:0000313|Proteomes:UP000037146};
RN   [1] {ECO:0000313|Proteomes:UP000037146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) 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:KMY49940.1}.
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DR   EMBL; LFZW01000001; KMY49940.1; -; Genomic_DNA.
DR   RefSeq; WP_049681292.1; NZ_LFZW01000001.1.
DR   AlphaFoldDB; A0A0K9GTG3; -.
DR   STRING; 1679170.AC625_10750; -.
DR   PATRIC; fig|1679170.3.peg.2405; -.
DR   OrthoDB; 335833at2; -.
DR   Proteomes; UP000037146; 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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   PANTHER; PTHR45528:SF14; SENSOR HISTIDINE KINASE CSSS; 1.
DR   Pfam; PF00672; HAMP; 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   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};
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:UP000037146};
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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..252
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          267..483
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   483 AA;  55026 MW;  7F1F764E3F7A3738 CRC64;
     MTIKNRFLTS YIGGIVIASV SILTILCIAF YVTTGSVPTP KTLYQSFTKQ RSLSPEEELA
     YVELRNIAKT NPEKLLAEDM QKNLQQIDQR SLGVVIRQDN EILYHSKELV EESLIVHFPS
     FNTNNIETKG TIDNAGRLYR YIKFDFYYSD KSKGSVLVLK KENSFLDFLT KWGIIIIIII
     LLASIAAMLF LNQLLRKTII KPLENLGQVM SEMRDGDLMI ESPAIPTNTA REVHELTANF
     QSMRAALLVS IQEQQNLENN RKELIASISH DLKTPITSII GYVEGLQDGV AETPEKQEKY
     LKTIHSKSLA LNKLIEELFL YSKLDAEAVP FYFERLKLAK FLSHMVEEFQ LYNREIQFVL
     NVAEDVYVYI DRMQMNRAIT NLIENSMKFK KTIEPLCMIV EVVVVDHIVE IVVKDNGQGI
     SELQLPYVFD HFYRGEEART STTGGSGLGL AIVKQIVEKH NGHVKIQSKL HYGTTVTIIM
     EKA
//
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