ID I0HUP4_RUBGI Unreviewed; 1217 AA.
AC I0HUP4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RGE_33920 {ECO:0000313|EMBL:BAL96731.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL96731.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL96731.1, 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 ---------------------------------------------------------------------------
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; AP012320; BAL96731.1; -; Genomic_DNA.
DR RefSeq; WP_014429591.1; NC_017075.1.
DR AlphaFoldDB; I0HUP4; -.
DR STRING; 983917.RGE_33920; -.
DR KEGG; rge:RGE_33920; -.
DR PATRIC; fig|983917.3.peg.3317; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_269051_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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 5.
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; 4.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
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; 4.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAL96731.1}; 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:BAL96731.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 390..443
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 444..517
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 522..574
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 575..631
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 647..699
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 779..831
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 847..1071
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1095..1211
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1068..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1146
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1217 AA; 131925 MW; 4E0ECAFB4808B38B CRC64;
MNNALDALNQ RLRQERLALA LLLLAVALAL GWARLRARDD ALAAEGDRLA DQAVAVRQVL
ALQVDAARLA LDTLRSSLVA SPGGGSERLR AFAGSTPVIG DVLRLDAGGR VVAASRAMPP
GSRIGPLPDT QRPELLYLRP PDQDELGRRR LLMLLAMPDG GWLATELDTA HARAVFGAVR
YASDMRVALA HGSGRLLLSE PPVADPASVD LTRSSPAFVA HRRSGRDTSV QRAHSALSTD
DRLFALATLG APRLPLDGNI EFATSRNVDA VLEPWRTQTL LVVAGFLAVS LVAAFGLALM
QRRQREAMDR LRVESERLEL ALRGADLGLW DNDWRLDHGT VNTRWCEILG LPPPDGRDMR
AVWLERLHPD DRDTVIAAEQ RHLDGRSPAY EVIYRLRHAD GRWIWVLDRG KVLQRAPDGR
PLRMSGTLLD IDKRMREQQA LAASERRLAI TLRSIGDGVI VTDREARVTR MNTTAERLTG
WPEVQALGRP LVEVFRIVNQ RSGETVPNPA EQVIATGRIV ELANDTALLA RDGRRLFIED
SAAPIPGDDG DIAGVVLVFS DVTERYVARQ ALRERERLLA GITDALPGPV ARLDLQGRYR
FASAAYREWF GLDPATVVGR TISEVLGEPL HQLGLPYLRR VRNGEVVRFD LPLKTTDGVQ
RHAFVTLLPD RDAEGRVVGH FAVTFDIGEL KRTEEALRAS ERRLRVLLDN LMTGVVVHEP
DLSVREANAA ALQMLGAANL QALLARSAED WEVVDEHGQP LAQDELPAMR ARRGGRRIAD
IVLGLRRPDG RQLWALCNAV PLHDGDGRLE SIVVAFADIT ARREAERLER RLRDTQKMEA
IGTLAGGIAH DFNNILAGIL GRLTLAREDA AASRPVHEHL DQAMQAGLRA VALVRKILEF
SRGETGAMTT QPAAPVVEET LGMLRAMVPP GVQLLAVLPA EPVAVRVDGT QLQQVLLNLA
TNAWHALPVT GGRVEVGLER LDATQVRALG EPALAEGPVA HLWVRDDGHG IAPEVMSRIF
EPFYTTKPVG KGTGLGLSVV HGIVQAHGGA IRVDSRPGQG STFHVYLPSP EAPEPAPPPA
AGETAAPRPV ASGAHVLLVD DDPIVAAVHG QLLRRAGYRV QVCDSGREAL ALLERSPTAF
DAVVTDHNMP DTSGIELARR IAEAAPRLPV LLCSGFVDDA LHAQAAAVGV RVVVPKEDAY
ERLAPALAAV LAEGGGS
//
