ID A0A0C4YPT2_9BURK Unreviewed; 1282 AA.
AC A0A0C4YPT2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RR42_s2919 {ECO:0000313|EMBL:AJG24500.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24500.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG24500.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG24500.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP010537; AJG24500.1; -; Genomic_DNA.
DR STRING; 68895.RR42_s2919; -.
DR KEGG; cbw:RR42_s2919; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000031843; Chromosome secondary.
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; 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 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
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; 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; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 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:AJG24500.1};
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:UP000031843};
KW Transferase {ECO:0000313|EMBL:AJG24500.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 381..452
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 550..773
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 791..913
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 941..1057
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1097..1201
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 509..536
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 845
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 990
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1136
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1282 AA; 138505 MW; D2DBF23E6BF0263D CRC64;
MMAASASGLL AAWRRRLATR AGLRRYAYAV LLVVTVCLLA GGAAQLVYEN DRANLGTRVE
SMLATNARLL GLWSGEQQRR AERIARLPEA LRFARPLLLA PAPGQPLPDG EAVARFERWV
TPVFQSSGYL GYVLATPDLK IVASELPGRT GRLLLPEPAQ TARRALEEGS AASPPYPAPE
RTRDPWGTLV DLPFQVVCAR LLDAGRAIGV LCLRLDPGAV MLPIIAAGQF GRTGELYAID
ARGRLVSPSR FGAELEAKGR LAPGTASMLN VWARVPGQSG KDGGGAQPGG PLTLVAERLL
RDHASVLAYD YADYRGQRAA GAGIWVPGLE MGLIVEQDMG EAFAPYLFTR DVLAALTAII
LLLIGTATWI ARRDGRRLAE SQERMRAMLE HSPAVMSLKD SDHTMLALNP AMQALLGASE
GEVLGRSDWD AGSNPEVARA RREMEARVMS SGKAEEHVYA LRTPHGERHL QMTRFPVRNP
ATHQVVGVGA VGIDITEQVE VNRRLTSLSQ TLERRVEERT RELAQTNAEL VVAKQAAESA
AHAKASFLAN MSHEIRTPMN AVIGMAHLAL RTRLDDKQRG YLEKIQHSGQ HLLEIIDDIL
DLSKIEAGKL EIERIDFSLE RMLRTVSDLV AERAVAKHLE LIVEVAPDVP DSLRGDPLRL
RQILINFANN AVKFTHQGEI VIRVERHGDG QCQPRIRLRF EVRDTGIGID PATCARLFQS
FEQADASTTR RYGGSGLGLA ICRRLVELMG GTLGVESTPG KGSNFWFELD LLAGKKRPAS
ALVAPQLAGC RLLVADDHDY ARQVIIAMLR NFGFRVDEAG SGRAALARIA QADEAADPYQ
AVFIDWKMPG LDGIETARHI DAMRLRHPRP RRVMITAHGR EEVLREGEQS GFDATLIKPV
SASLLLEATV RTLSPDNDAP PEATQPHSAA LDATPELPSA RVLLVEDNDI NREVAVHLLQ
AAGIYPDTAE NGAVALHLLQ SGAYDLVLMD VQMPVMDGFE ATRHIREQEA FASLPVVAMT
ANALPEDRAR CLAAGMNDHI AKPISPPAFY AMLRQWLAVP GGDDAAPSAG SRPAWVDALA
SSPHLDVGGG LGRVSGRAQV YRQLLERFAS GYADMPERIG ERLAHGDRDG ALSLAHSLKG
LAANLGAMPI SSAAATLEAS LQLPHAPGRP DPVTLLAALR TAFLPLLAAL RTHLPTEPAA
LDGGAPDACG PLAGPDVKQE SVLKLLREQL EEGDSAANNT FARYRDVFTR LLCADGCQRL
QAQVERYDYL AALATLDGGA AS
//
