ID A8TM42_9PROT Unreviewed; 878 AA.
AC A8TM42;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BAL199_02479 {ECO:0000313|EMBL:EDP65654.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP65654.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP65654.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP65654.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EDP65654.1}.
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DR EMBL; ABHC01000003; EDP65654.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TM42; -.
DR STRING; 331869.BAL199_02479; -.
DR eggNOG; COG0642; Bacteria.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:EDP65654.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW Transferase {ECO:0000313|EMBL:EDP65654.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 611..729
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 661
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 878 AA; 93783 MW; 3479FBA7EA888C79 CRC64;
MVVRLVDRLS LRGSIIALII AIGVIGPLAA GWVHHSQLVS RARAAAERTV AAINAEKAFQ
VSASVNEAVS LLGIIEHDVE GHLSSIKNST SGRLDEVFVL DGETGEVLES TDRAQLNKIR
SEETYFNAGR QGLYIGPPVY DLYRRKSVST VAMPARRNGR LLVLGAVLSP VGFAKVLQTK
STAFKSEDSY LISSGNLLVS PPRLAADTGA LVGGVHETFV NRCIAGQSAV EDGTDYRGVA
VIVSYRWIET PAACLVTQID IAEFDETLSG VAASTALIAL AVVGGSLVAA FLVFAPLFRR
ISNAVKVFHS VSDGDTTARL TPSVYRELQT VTQGFAMMVE ERSRSEDELD AARLEAETAN
RTKSRFLAAI SHELRTPLTG VLGMLDLTER RRSLAEVRHD IEEARTAGRH LLSLINQVLD
FSKIEANKIE LTTKPFDPEA LIRNAAGLFE ATARAKGITI ETERTGILPE ALVGDAERLA
QVLFNLVGNA VKFTAEGRVT VRYGTEPSGT RCHRLRVEVI DTGPGISSEG QALLFREFSQ
IDRLDAPSAS GTGLGLAISA GLMTRMGGNI GVSSGGTGTG STFYIDLELE EGDRLASVES
KTGQIPSRPL VILLADDVPL NRDIIAQYLT EEGHTVDTVG DGVACLERLR SGTQYDAVLM
DVNMPVLDGV EATRWIRAEA TTWSQIPIIG LTADAFTEQR DAYRMAGMTD CLPKPIEWDQ
LLSALASVTG VAGASIGDSQ PVSVPVGLSS AQDLEAVELL SAKQQGDLMA RLGHGRTVSL
THEVLTTIEE QVDQMASLAD DPERVRAIGH AVRGVSGNVG LTRIASGAGL IEAAARADQI
DVALINALRD AVAATRQRYA AFAEQTSTPH LEAIRETP
//
