ID L0D790_SINAD Unreviewed; 1157 AA.
AC L0D790;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sinac_0285 {ECO:0000313|EMBL:AGA24735.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA24735.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA24735.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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};
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DR EMBL; CP003364; AGA24735.1; -; Genomic_DNA.
DR RefSeq; WP_015243920.1; NZ_AHZQ01000548.1.
DR AlphaFoldDB; L0D790; -.
DR STRING; 886293.Sinac_0285; -.
DR KEGG; saci:Sinac_0285; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_000445_127_0_0; -.
DR OrthoDB; 9762493at2; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0016020; C: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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGA24735.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 480..700
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 765..878
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 887..1003
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1033..1155
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 380..470
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 814
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 936
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1088
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1157 AA; 127656 MW; 190C84BD9464AFA5 CRC64;
MIDKKTAIAS RRRSGTSLLI GVAAVLLVFV VSGTVSYLNT RTLDRDARQV THTHEVLSAL
GELLSLMKDA ETGQRGYLLT GDDRYLEPYS SALARIDQRM GKFEGLIRDD SDHRTHLPAL
KANINTKLEE LAETVELRRT QGFEAARATM MSDRGKAAMD ALRTLIQSMQ EDERIQRALR
IAEMDNAYRV AIGSGILTGV LGALLSVAVG SLLRQAMLTR QRQDWLQSGQ IGLAKAMAGE
QRLEQLGESV LKFLADYLDA HAGVFFAKNG SGFRRVATYG VPALDGTPAG FEPGDGLLGQ
AVKDGRAILV RDVPDGYLTF GSALGHGKPR HLVIAPVAAD DAVKGVLELG FVHSLDGRMI
TLLDTVSSLV GVAVKSANYR THLQNLLEET QRQAEELQAQ GEELRVSNEE LEEQGRALKE
SQVRLEHQQA ELEQSNVQLE EQTAILETQR DDLLQTKEAL QLQARGLEQA SRYKSDFLAN
MSHELRTPLN SSLILAKLLA DNPQGNLSEE QVKYAQTIRS AGNDLLVLIN DILDLSKIEA
GRMEVRPEPV SLAQLVDDLR RTFEPVAAQK GLAFHTLVSP ACPETINTDC QRLEQVLKNI
LSNALKFTEQ GEVKLNVSRA ADGRISFAVT DTGIGIPEHQ HQVVFEAFRQ ADGTTNRKYG
GTGLGLSISR ELTRLLGGDI RLATESGRGS TFNVTIPELY SPALVRPRDI STTVSAAQVA
AEDRGASLPA IPPVFPRERA NRLSAPSRAR QMDDDRERLA GGRRIILAVE DDESFARILY
DLAHELDFQC LIATTAEEAL AVAVQYLPNA VVLDVGLPDY SGLSVLDRLK HDARTRHIPV
HVVSAGDYAQ TALSLGAVGY MLKPVKREEL VEALKQLETR LAQRMRRVLV VEDDPVQLDS
MRRLLDSVDV ETVGAGTAAE CLEQLKEATF DCMVLDLSLP DASGYSLLET LSREDAYAFP
PVIVYTGRDL PADEEQRLRR YSNSIIIKGA KSPERLLDEV TLFLHQVVSE LPPEQQRMLE
KARSRDAALE DRRILVVEDD VRNVFALTSI FEPRGAVVQI ARNGREAIAL LEDSLADHQP
KIDLVLMDVM MPEMDGLTAT REIRQRPEWK KLPIIMLTAK AMKDDQARCL EAGATDYMAK
PLDVEKLLSL VRVWMPR
//
