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Database: UniProt
Entry: A0A1I4JGQ2_9BACL
LinkDB: A0A1I4JGQ2_9BACL
Original site: A0A1I4JGQ2_9BACL 
ID   A0A1I4JGQ2_9BACL        Unreviewed;       599 AA.
AC   A0A1I4JGQ2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN03159341_10894 {ECO:0000313|EMBL:SFL65742.1};
OS   Paenibacillus sp. 1_12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFL65742.1, ECO:0000313|Proteomes:UP000198699};
RN   [1] {ECO:0000313|EMBL:SFL65742.1, ECO:0000313|Proteomes:UP000198699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_12 {ECO:0000313|EMBL:SFL65742.1,
RC   ECO:0000313|Proteomes:UP000198699};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOTE01000008; SFL65742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4JGQ2; -.
DR   STRING; 1566278.SAMN03159341_10894; -.
DR   OrthoDB; 2491077at2; -.
DR   Proteomes; UP000198699; 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   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; 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:SFL65742.1};
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        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          316..369
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          486..598
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   599 AA;  68252 MW;  BFC0CE95529D48F0 CRC64;
     MKAFLVLRKL SIKMKMVLAF LSVSVLSVLL LGLLSNYYYS KAVEKEFFTI SNEATARLNY
     HLDYYYQQLQ QSTQYLIQND TVQEWLTSES YTNLDKQNVE KELRRYLALN YSEIQGMFLI
     SKSNQIVSMA QYFGKLDRFN DEPWYGRPVS PNIRILPTHT AKYEGAYGRP VMSVLLPIYN
     KETIELIGTL AVDISLQEID RSFKSSQLAK SGIFFILAGD DSIVYHPNEE LNGLQKRQTE
     LAALKIPDKG ETAIQRFRGD DYLIGSSLSP VTGWRIVSLV PFAEVAVGLS TARLSMMLVL
     VIITCLVILV VPLLSNRFVD PILTLRGLMR QVAKGDLSVQ TESVPGQDEL QQLFHSFNIM
     VKRLDELIVT NSNLQMKEMQ ALLQQKETLI KALQNQINPH LLYNTLGIIT SMAYLEKVPV
     IERMARNLAD VYRYTAQFTD MEVYLEEELG QLRKYLDIIH VRFPKHFQSR YFINEKFIRC
     RVVKFILQPI VENAVKYAIE PRGGEGVVIV SAYDEGRDLI IEVADNGPGI GDAELKRITE
     QLEMISTKVE QNYAQQDSLG LANVHARLVL QYGNKYGIKL SSFPGRGAVV SIRIPIHLE
//
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