ID E1T4Y7_BURSG Unreviewed; 774 AA.
AC E1T4Y7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BC1003_1317 {ECO:0000313|EMBL:ADN57293.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN57293.1};
RN [1] {ECO:0000313|EMBL:ADN57293.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN57293.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002217; ADN57293.1; -; Genomic_DNA.
DR AlphaFoldDB; E1T4Y7; -.
DR STRING; 640512.BC1003_1317; -.
DR KEGG; bgf:BC1003_1317; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_363586_0_0_4; -.
DR OrthoDB; 9797243at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADN57293.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ADN57293.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 192..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 457..672
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 774 AA; 85498 MW; 8A8376A8BEEB7098 CRC64;
MQADFIMRAA MWQRVLFMCF MWWSTHAFGA GLSSTSGDEQ HALALSPVQA FEDVSGKMPL
QDIAALSENN PRSFVTVSDK RLKPGFTRSA WWLHVDVSNR GLTAVPLVLA LLDTRLEHVD
FYVKRSGDWT PSNSSPADAA SSQVLSRYPQ MEFTLAPGER LPVLIRVTSN TALALEPMLY
STAAFNALER RAALWDGGLI GGTLALAWCA LLIAYFSRSG SFLVLAAMCF MTALYDAADR
GYTKIYFWPH ATDWNSRSVT VFGCTAVFLF IVFILRMATN EKASLPARYI LLSFALLECI
AAAGAAFGNL FVFVQLGMYG NALFGIVQIG VAATLARRST PTARIMLLAV IFALFNFALR
MLETLGSLPP GLLWLKSDIH PNPVVSVIGL ATHLIVLAAW INHVGKQRLA ARAELADWQR
TEHDRLREQV ERRTLELNEA LLYAEERNQQ KIETLGYVSH DLRAPLATIS SYARLLLNAA
DSKQSTLIHA IERSVNYQLG LIDELIGYAK AELQPLDTAP TETDLPSLLD DIAEYAVALC
APLNNQFHYQ ALTSLPRRLT IDGRRLQQVL LNLLSNASKF TRDGTVMMTV RARRRGRHWH
MGFEVADTGI GIELEEQSKL FTAFRQIQSV NGSTGLGLFI AQRIVNTMGG ELRVASAPRE
GTSFSFELIV AIADDCEASP LNVVPFSSSA STSARLHTRR PLHDAVPPDS ERRQLAVLAK
DGRLTDIEQW IENMLALHPS CAAFLTEVRH FVEALDFAGV EALALTPHET TNVS
//
