ID A0A017HMP9_9RHOB Unreviewed; 893 AA.
AC A0A017HMP9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Rumeso_02916 {ECO:0000313|EMBL:EYD75570.1};
OS Rubellimicrobium mesophilum DSM 19309.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD75570.1, ECO:0000313|Proteomes:UP000019666};
RN [1] {ECO:0000313|EMBL:EYD75570.1, ECO:0000313|Proteomes:UP000019666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD75570.1,
RC ECO:0000313|Proteomes:UP000019666};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (FEB-2013) 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 -!- 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:EYD75570.1}.
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DR EMBL; AOSK01000075; EYD75570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A017HMP9; -.
DR STRING; 442562.Rumeso_02916; -.
DR PATRIC; fig|442562.3.peg.2870; -.
DR HOGENOM; CLU_000445_114_51_5; -.
DR Proteomes; UP000019666; 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; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019666};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..201
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 278..331
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 417..469
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 521..741
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 762..873
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 873..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..505
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 812
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 893 AA; 96551 MW; 114EDB7B11A55915 CRC64;
MAGLALGRAP GLLAALLSAT AAGTLFMEPG PLLVPAGGDQ ALVLALFLLV TITTALAFDA
LFGAFEDLER RAVLLREGEA RFRALVESAP KKMWVNRPDG SGDIYNAAWR DFTGQGDDHQ
GRAWIEAIHP DDRTIVVSAR EAGIRERRAY NVEVRLRAGD GRYRRHRAQV APLLRDGAIE
SWVGIATDIE DLRSAVERLR EGEERLRLAT EHAEVGFWDV DLVQDRLIWP PRVKAMFGIS
AEAEVSMADF YAGLHPDDRE ATTAAFLRAC DPEMRGLYDV EYRTVGKEDG VVRWVAAKGR
GLFDEAGQCR RVVGIAIDIS PRKADEQRLR EYADELETLV DAVPAAIWIA RDPEARRVDG
NRVARDLLRV PSPANMSKTS PDARDAVRHF RILEPDGAEI PPRDLPVQRA ARGVQVRDFE
ETVVFEDGGA VHLIGNAVPL LSSEGRPRGS IAAFVDITAL KQAESGLQAA NETLERRVDE
RTAELREANA RLARETAERL RAEADLHQVQ KMETIGQLTG GVAHDFNNLL TPIMGSLDII
RRRVTLDQRT DRLLGGAMEA AERAKTLVAR LLAFARRQTL ETRPVDMGQL VDGMRDLIAR
SLGPQIALAV GIPGALPPAK VDPSQIELAI LNLCVNARDA MPEGGSLRIS AREELVAEGS
RTDLAPGDYV VLSVADTGTG MDATTLQRAV EPFFTTKPRG RGTGLGLSMV HGLAAQSSGA
LLLDSQPGQG TRAEVWLPAA QEAAAGRRSE DVEAIPAPFE AKVLLVDDED LVRLGTAEML
RDLGYVVAEA NGGAAALELL RGGLAPDLLV SDYLMPGMNG ADLATAVRHL RPSLPVLLIT
GYAQLADGAA DDLPRLTKPF RQSDLAHRVA DLLSPEAHGM TPGSSRSPDL GAP
//
