ID D4H1R1_DENA2 Unreviewed; 1005 AA.
AC D4H1R1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dacet_2058 {ECO:0000313|EMBL:ADD68821.1};
OS Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Denitrovibrio.
OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD68821.1, ECO:0000313|Proteomes:UP000002012};
RN [1] {ECO:0000313|EMBL:ADD68821.1, ECO:0000313|Proteomes:UP000002012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12809 / NBRC 114555 / N2460
RC {ECO:0000313|Proteomes:UP000002012};
RX PubMed=21304711; DOI=10.4056/sigs.892105;
RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT (N2460).";
RL Stand. Genomic Sci. 2:270-279(2010).
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 ---------------------------------------------------------------------------
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; CP001968; ADD68821.1; -; Genomic_DNA.
DR AlphaFoldDB; D4H1R1; -.
DR STRING; 522772.Dacet_2058; -.
DR PaxDb; 522772-Dacet_2058; -.
DR KEGG; dap:Dacet_2058; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_104_15_0; -.
DR InParanoid; D4H1R1; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000002012; Chromosome.
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 CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADD68821.1};
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:UP000002012};
KW Transferase {ECO:0000313|EMBL:ADD68821.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..500
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 516..641
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 668..784
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 823..916
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 238..272
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 570
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 862
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1005 AA; 114122 MW; BAAF435BD662D122 CRC64;
MRIQTINAII TILSLVLLTY FSVLLIDLSK KTKAAEIRNN LSNELSMQMN DLVILIYEIV
LFDSKQAKTK WLDKYAQTTQ TVEKLTESPA PKLLARKMHI KMLHELLKNV FTEYLKIANK
TGNDNYYKYQ IDIQTSNIFS ISSELNKNVL VLQKQTVTEL SNLTQKVNKE VLMFIFSLTI
FLIMAFIFLW KRVIRPIVFI SKILPEYAIG SDLEPLKWKY NDEIGIFVNT FNDTLEKRNE
WENELTLINR QLLNTNKDLA KARDAAEQAS KAKSSFLANM SHEIRTPLNG IIGLTKLMLD
LELSNKQKDY MRKIDRSAKA LLGILNDVLD LSKIEAGKLR IDNHDFVFES VFKSIDDLFT
IKIEEKGLEL FFEIDPEIPQ HLTGDPLRIK QVLINLVSNA VKFTDEGEIH IKAEVTEITD
SDISILFSVR DTGVGIPANE LEKIFTAFTQ VDETSTRRYE GTGLGLAITK NLVSMMGGTV
TVESDINMGS IFSFKLTLQI PVNAVSSNPN NLYGMKTLVV DDKETSREIL RKILESWSFE
VYTAKDGESA LKLAQAEHEK GSPFHLVLVD WKMPGMDGFE TAEKIREFSR DSGIHDKIIM
IMVTAYEKEL TEKMSGNDNF NFVLSKPVTP SILFDSIVNI QYPKNSAEAE TYNEVAKAYP
GNDIGGKSVL LVEDNSVNRL VAQETLQKFG LTVEVALNGK DAVEKVKSKK YDAVLMDIHM
PVMDGYRATA EIRQIFDKKQ LPIIALTADA LDTHKEKCFA VGMNDHLSKP INIEILFKVL
CKWLQVDYEI QEMRPSDEYF QQLTKNKITC LDIESAGKRI NYDWELLRAA IATFRNDYKD
AATTLNKLME NKQFEQAEIF LHELKGAAGY IGAVTIVKMA IDLRQALLDE KLDSTTLLTQ
ELCSELDNVI ININNIDADT YQSSNNIQCS DQRIKQVFST VLDIISNFKL VPDETMTELS
SVLQSYPIIF EKLESEINDF DYSKAEVTLK KATLQLGIDM EESDD
//
