ID I0HP53_RUBGI Unreviewed; 1233 AA.
AC I0HP53;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, 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=RGE_14490 {ECO:0000313|EMBL:BAL94790.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL94790.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL94790.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP012320; BAL94790.1; -; Genomic_DNA.
DR RefSeq; WP_014427659.1; NC_017075.1.
DR AlphaFoldDB; I0HP53; -.
DR STRING; 983917.RGE_14490; -.
DR KEGG; rge:RGE_14490; -.
DR PATRIC; fig|983917.3.peg.1415; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_001896_0_0_4; -.
DR Proteomes; UP000007883; 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; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 NCBIfam; TIGR00229; sensory_box; 1.
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; PF01627; Hpt; 1.
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; SM00091; PAS; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAL94790.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW Transferase {ECO:0000313|EMBL:BAL94790.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 386..456
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 457..508
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 576..627
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 663..878
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 904..1018
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1062..1156
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1023..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 618..649
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 953
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1101
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1233 AA; 132756 MW; E738D1FF50AA53F5 CRC64;
MPPDSAGAPR RSRLTALRVA LGYAGLASLW ILLSDRWVEH LMTDAEARVL AGIAKGWVFV
AVTSLLLYVL VRRMAPAEPA SGRPQRGERV LPALVAASIV LLTAAGLALA LRQQHRSTEQ
TLRSIADLRS AQASAWAAVH LADGGRVREI QPSQLQARLE LLRAERGYAA VALLDAQWRS
VWSSGPAPDA PQDAPDLHPD KPRLLGPQLD AEGLPHLLLL VPLAPGQAPA GGYALLQLAA
ADLPPLALGG MTMEGAATVL VRRDGNDLVY FGAPARKGFA IWRRPADDSA IAATSHPAGT
LIDGGDERGE AALGLLGPIA GTPWQLLTRV DHTVIERQRW QAASGVLLAA LLAGFGATGL
LALRRQREAI DRHEAERLRQ AERVEALAVF EAIADSSPDM IFAKDLQGRF LLFNRGAERF
TGALREQMLG RDDSVLFPPD IVAGLRAADR RAQEGVIELE ETLPTPDGPR EMTVTKGPLH
NRAGELIGVF GVSRDVTDLR KERALLAETS RIARIGGWSY DDRTRRVTWT DEIRRIVEVD
GEIDPGIGFA LGFLGTESRE QLQAALQANR EHGVPLDLEL PVQTARGRER WVRIVGQLEF
EGRRVLHAQG FVQDVTEAKT LRIELDRHRA ELERQVRERT ADLEVARARA EAGMRARDAF
IRIISHELRT PLHQILNLAP HLHRDDGSPE DAFVDAADRL AEILEDVLTL SELEAGGVVP
RSADFELGAL LHQAREQVEA EAQRKGLALT VDAGSVPLWL RGDPAMLGRA LGNYVRNAVK
FTAEGSVQII ARRVAEDAEG VTLLLEVRDT GPGIDPAQQP RLFGAFEPGD LSMTRRHGGA
GLGLALTRRL AELMHGQVGV HSRPGRGSRF WLRVHLPRGR DVSTRPPGQL TVEATLRARH
AGTPVLVVDD DPVNRESASA LLGAVGLKVL LAENGHEALE RLAADQPALV LMDLQMPELD
GLGAAREMRR RGATLPILAL TASDADQTLT ECLAAGMDHH VHKPVEPRAL YETLLHWLGS
GAADADETEQ DTGAPHPAPA EAALPPLPGV DTVDALLRSG GSGARALALL RLFVRTHADD
SPQLETLCAE GRWSQLRQLS HALRGAAGNV GAREVHLAAT RLEALLDEQA PVASRQEATR
VLSAALAELI DGVRSLPEPE APAAPSRSVG DPGVAVAGLA LLLTSGDTAS ASFIAEHEPE
LRQSLGAEFE HLNDLVESFR FDEAASLLAR HAA
//
