ID A0A0D6B8P7_RHOSU Unreviewed; 851 AA.
AC A0A0D6B8P7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NHU_04303 {ECO:0000313|EMBL:BAQ71416.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ71416.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ71416.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ71416.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP014800; BAQ71416.1; -; Genomic_DNA.
DR RefSeq; WP_060836333.1; NZ_AP014800.1.
DR AlphaFoldDB; A0A0D6B8P7; -.
DR KEGG; rsu:NHU_04303; -.
DR PATRIC; fig|35806.4.peg.4401; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000064912; Chromosome.
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; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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; 3.30.450.20; PAS 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAQ71416.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:BAQ71416.1}.
FT DOMAIN 339..560
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 577..690
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 719..838
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 7..52
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 624
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 768
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 851 AA; 94647 MW; AC62B0A5C52E8C8E CRC64;
MDLHDKLARE RRARLAAERL LERKSRELFD ANRRLALQAR ALSEEVDQTR QAADELRGCN
DKVMTELAEV SKAFTVAKQR LWDSLETVRD GFALFGADDR LVIGNKAFFD LFEGLEEVIP
GIRYDEIIRL AVEEGVFDIG QERPQEYAET LLSRWHLDPV PPRVVRLWTG EYLKLTDRRT
PSGDMVCLAI NITDMMRMWA ALEAIPDAFV LYDAEDRLVM CNDRYREFYA ESAQSMVPGA
RFEDILRQGL ENGQYPEAIG REEDWLTERL VNHQKASSPV EQRLADGRWL RIFEQRTPDG
GIVGLRVDIT EQKRQQEALE QARVAAEAAN RAKSAFLANM SHELRTPMNG VVGMAEILCE
TEMSEEQRLY AHTIRESGEA LLGLLNDVLD YSKIEADKLT LNPAPFDLER IIHEVVTLLQ
APARDKRLDM LIDYDIFLPT RFIGDGARLR QILTNLVGNA VKFTEEGHVL VRVVGFEDAS
GRYQIHLIVE DSGIGIAPDL QEHIFGEFNQ VDDQENRKFE GTGLGLAITK RLIEMMEGEI
WLVSGKGEGA CFGIRLTLPV CEEADALPAA PATRARRVLV VDDQEVNRTI LERQLGQLGL
EVVSHICGEL ALQETGRFDL VVTDHRMPGM DGMSLARALR DGGYDGPILM LSSNPTRMRA
ADDPVASGVD LVLQKPLLRR SLYEAVAQLA PPAAGQPARL PAPPAPAGVP VAPDAVPMRI
LAAEDNRTNR LVLEKMLDGL VLDIRFVKDG DEAVAAFSEA RPDLILMDIS MPGCDGKEAT
RRIRALEAGS DLAPVPVVAL TAHAMIDDVD AILAAGLNGC LTKPLRKAEI VETLEAYRPD
RCLPIRLAGM G
//
