ID Q0RBV2_FRAAA Unreviewed; 1340 AA.
AC Q0RBV2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=FRAAL6455 {ECO:0000313|EMBL:CAJ65078.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ65078.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ65078.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ65078.1; -; Genomic_DNA.
DR STRING; 326424.FRAAL6455; -.
DR KEGG; fal:FRAAL6455; -.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_3_0_11; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 7.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 4.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 6.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 7.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 4.
DR PROSITE; PS50885; HAMP; 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ65078.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 60..107
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 147..199
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 239..291
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 331..383
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 423..475
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 515..567
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 607..659
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 911..1139
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1216..1333
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1139..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 832..901
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1266
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1340 AA; 142224 MW; DDC1EB800B39091A CRC64;
MYGRDAGLVT LTLLQKLRTD LDIDRGGSRK GAGTVGDRLE ATVTEVTDRE AARARLDDPA
LRQLLAGLTA VRGGDFGTRL PRVGDDLLDE IATVFNGMID QLALFTSEVT RVAREVGTEG
KLGGQAEVPG VSGSWKDLTD NVNAMAGNLT GQVRDIAQVA TAVAKGDLSQ KITVDARGEI
LELKSTINTM VDQLSGFADE VTRVAREVGT DGRLGGQADV KGVSGTWRDL TESVNVMAGN
LTSQVRSIAQ VATAVAKGDL SQKITVDARG EILELKSTIN TMVDQLSGFA DEVTRVAREV
GTDGRLGGQA DVKGVSGTWR DLTESVNVMA GNLTDQVRSI AQVTTAVARG DLSQKIRVDA
RGEILELKET INTMVDQLSG FADEVTRVAR EVGTQGNLGG QANVRGVSGT WKDLTDNVNV
MASNLTAQVR SIAQVATGVA RGDLSQKITV EAKGEVAALA ATINTMVDTL GAFADEVTRV
AREVGTDGRL GGQASVKGVS GTWKDLTDNV NFMANNLTSQ VRNIAQVTTA VARGDLTRKI
DVDARGEILE LKTTINTMVD QLSSFAAEVT RVAREVGTDG ILGGQAEVEG LSGTWKRLTE
NVNELAGNLT RQVRAIAAVT SAVATGDLTR SIDVDAQGEV AELKDNINAM VRSLRETTRA
NQEQDWLKTS LAHIGGLMQG HRDLQTVAQL VIDELTPMVD AQYGAFLLAE SGVDRPALNL
IASYGYQAPW DVPRRFDFGQ SLVGQAARTK RTIVVANTPA DYLQIASSLG QSAPVALIVL
PILFEDQVLG VIELASFSPF AQVHHDFLNL LTETIGVNVN TIIANARTDS LLDESQRLAS
ELRARSEELQ SRQEDLQLSN AELEEKATLL ARQNHDIEVK NFEIEQARQE LEERARQLAL
ASKYKSEFLA NMSHELRTPL NSLLILARLL AQNPTRNLSP KQVEYAHVIH SAGSDLLQLI
NDILDLSKVE AGKMDVHVEE VALVDIVDDV QATFSPITAE KGLRFTVAMA PDLPARLRTD
RHLVAQVLRN LLSNAVKFTE QGSVDLAIAV SGAGAGGRAP GQAVLFSVSD TGIGIAAENL
ERIFGAFQQG DGTTSRRYGG TGLGLSICRE VATLLGGEIQ ARSEFGRGST FTLQLPMAPA
ATTSSDGPQP AAEQPAAVPP SPRAALPAAT PVDEAKPGLH LVTATAAAPT TASTLVDPGP
SPAPEVAGAP GIAGRTVLVV DDDVRNVFAI TSILDLYGLR VIHAADGRMG IDALRSNPGI
DLVLMDVMMP EMDGYATTTA IRAMPQFADL PIIAVTAKAM PDDRQKCLDA GATDYVTKPV
DIEELLACIR AGLAPGGHPR
//
