ID G2LKB4_CHLTF Unreviewed; 977 AA.
AC G2LKB4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cabther_B0603 {ECO:0000313|EMBL:AEP13601.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP13601.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP13601.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP13601.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(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};
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DR EMBL; CP002515; AEP13601.1; -; Genomic_DNA.
DR AlphaFoldDB; G2LKB4; -.
DR STRING; 981222.Cabther_B0603; -.
DR KEGG; ctm:Cabther_B0603; -.
DR HOGENOM; CLU_304163_0_0_0; -.
DR Proteomes; UP000006791; Chromosome 2.
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; cd12914; PDC1_DGC_like; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEP13601.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006791};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..536
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 592..825
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 850..965
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 538..576
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 901
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 977 AA; 106300 MW; CCB08A15B49E60F5 CRC64;
MKATFPLWKL DVPAALAALV AGGLGLGLNA FPLSIGSDLH FIFGPIFPLI IALTFGPLYG
MVAALLAGLA TVWLWVHGLA LPFLVAQAFV VGWCVRRWKW RALFADAVFW VGISPLLYFL
HVRSGVYPDG LGPAVAFKYV VNGLLCTTLA DSSLGWPAFG RLLARYGARL PENTMAARLT
RVLTLVAVVP ACALAVWYAH AASDQQEQEV RAELTTQTRF VANVLSDKLL VARQDVIILA
NRLSEMPDDP AAVARRLQRY HQHAFLFETL LVADTAGKVI ASSPVVSEPQ LNVAGHPYLQ
AALSGQNVVI SDGLHCPVPA GKDPCIAFAA PIRLLDGSVR GVVEGRMTTT QLSRLLSGSV
AHRGEPFHLV VLDRQSQVLA TNRPDLFPLL AKTRLSDIRA YDRALWLPVP ASGQEARFWV
WQEREPETGW QCYALVPFAV VHQRAATVFI PFLLAIPFVL FVVAWASGVT VRRVMRPLDE
LTATARVLAA DPERAPDILP DSPNGQTLPA TQLPAEIAHL TEAFHAMARQ VGKTMSYLRA
TNIELEIARQ RLEDARDNLE RELAARTAEI ERREEARLRS QKLELLGHLT GGIAHNFNNL
LTVILSYSSL ELSRRAPDDP ACKGLQSIRR AAERGRDLVK QLMAYSRASE ASAALCFPLH
DALRTVQGMV ERLFNEEVEL TTNFAAGEVF VYAIPQELEQ VFLNLLVNAR DAMPNGGTIS
LETTLVADTA AEAGGVVFPA GSRLEELLAA QPVVRISVRD TGTGIPPEVM ARLCEPFFTT
KEQHKGTGLG LSTALGTITS AGGLLRVESE VGKGTAFHVY LPVAEQPASG VPTSGSHRLS
FLKPSAQAQR VLVVEDDPDV RATVGAALLA GGFAVVEARD GQAAWNIIQQ QAGRFDLVVT
DVRMPNVNGV QLASSIWETY PDLPVLFISG YADRDDTRQS FAFRDNLIYK PFTATEIVEK
VKSMMDKNTA EQPTKVG
//
