ID U5N9L7_9BURK Unreviewed; 1405 AA.
AC U5N9L7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cenrod_1932 {ECO:0000313|EMBL:AGX88010.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88010.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX88010.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX88010.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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};
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DR EMBL; CP004885; AGX88010.1; -; Genomic_DNA.
DR RefSeq; WP_022774700.1; NC_022576.1.
DR STRING; 946483.Cenrod_1932; -.
DR KEGG; cbx:Cenrod_1932; -.
DR PATRIC; fig|946483.4.peg.1947; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3284; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_254024_0_0_4; -.
DR OrthoDB; 5519028at2; -.
DR Proteomes; UP000017184; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 5.
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; 5.
DR InterPro; IPR007891; CHASE3.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 3.
DR Pfam; PF13426; PAS_9; 2.
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; 5.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
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:AGX88010.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW Transferase {ECO:0000313|EMBL:AGX88010.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..238
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 264..316
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 411..461
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 469..533
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 551..603
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 611..675
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 693..745
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 753..808
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 824..876
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 901..1117
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1139..1256
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 311..341
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 867..894
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1191
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1405 AA; 152549 MW; 0DBE358F2CF55041 CRC64;
MKDAETGQRG YLLSRNGAYL ERYLAVTNDI SGNLHELRRM AFISGSHKHL DTLEPLIHEK
LQEMARSIQL RRDNDQNGAL ALFNSDDGKR IMDAIRAEFI QFNRVESDSL EQLNAKANAE
LSRSFVLVTI SSMLALLFAI AFASLIHQQT QQRIKSLLLI ETRQLLDAQD VANAQLRHAN
FTLQVSEAKL TVTLNSIGDA VIATDAEACV TLLNPAAELL TGWTNAQANG RKVDDIFHII
NKVTRQPATI PVTAALTCGT MQGLLNHTVL IARDGSERDI ADSCAPIRDS DGNVVGAVLV
FRNVSEEYAA QRVLSKQREE LEAQNEALSS SQAELDSSRA RYFDLYDLAP VGYCTLSIDG
RIMESNAAIA TLLGQEQTSL NGQFFSKFLL ETDADSFHVL KNRLTKTSAQ ETVEFQLRGK
DGRPFWAYLT GTVAQDEGQT VLHFAIIDIS ARKQAEDALL QAGALQSAIF NSANFSSIAT
DAQGVIQIFN VGAERMLGYT ATEVLNKITP ADISDPKEVI TRAETLSAEL DTPITPGFEA
LVFKASRGIE DIYELTYIRK DSSRFPAVVS VTALRDAEGA IIGYLLIGTD NTARKQAEEA
LLKAGALQSA IFNSANFSSI ATDARGVIQI FNVGAERMLG YTAAEVMNKI TPADISDPQE
VIARAKSLTT ELETPIAPGF EALVFKASRG IEDIYELTYI RKDGTRFPAV VSVTALRDAE
GAIIGYLLIG TDNTARKQIE AEQEQLAQRL RDHQFYTRSL FESNIDALMT TDPSGIITDV
NKQMEALTDH TRDELIGAPL KNYFTDPDQA DQSIKLVLSE KKVTDYELTA CARNGQETAV
SFNATTLYDR NRKLQGVFVA ARDVTERKRL DQVLREKNLE LEGAKSAAEK ANLAKSTFLA
NMSHEIRTPL NAVLGLAQIG MRDGAGSQAS DTFSSIADAG EHLLGVINDI LDISKIEANK
LQIENRPFAL LDVMEGVMSF VTGRAKDKGL SLRVSLASEL PEWVEGDGLR LAQILTNLLS
NAIKFTATGV VTVAVERDGD DTDFRITDTG IGMNDEQRAR LFHPFEQADT STTRTYGGTG
LGLAISMNLA RLMAGDISVE SVLGRGSSFT LHLRLPAVAA VEDAAGVSPT VGCGLSGLSV
LAVDDVAVNR MLLEDLLVHE GAHVVLAEHG QQALDCLQQA GAAAFDVVLM DVQMPGMDGF
EATRRIRLMA PALPVVGLTA YALAEERAKC LASGMVDVVT KPINLKVLVD AIRRQTQPSR
WKAFEDERPA PGFVASAAPV PAAMATESAL VAVSAVDWPM TLLRHHGRHA FVKKLATAMH
EHFAEMPTQL RGAARDGDRE AMALMAHSLK GFSMEAPQLH ELTKTFEAVM RGGDAIQAGT
VETLACALEA VLAELVHRSQ QDGDA
//
