ID B6A1T9_RHILW Unreviewed; 2099 AA.
AC B6A1T9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rleg2_5393 {ECO:0000313|EMBL:ACI58573.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OG Plasmid pRLG201 {ECO:0000313|EMBL:ACI58573.1,
OG ECO:0000313|Proteomes:UP000008330}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI58573.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI58573.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI58573.1,
RC ECO:0000313|Proteomes:UP000008330};
RC PLASMID=pRLG201 {ECO:0000313|EMBL:ACI58573.1};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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; CP001192; ACI58573.1; -; Genomic_DNA.
DR RefSeq; WP_003591282.1; NC_011368.1.
DR KEGG; rlt:Rleg2_5393; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_3_0_5; -.
DR Proteomes; UP000008330; Plasmid pRLG201.
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; 11.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 7.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; 10.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 11.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
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; 12.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
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:ACI58573.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:ACI58573.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACI58573.1}.
FT DOMAIN 117..174
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 214..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 306..358
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 398..450
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 490..542
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 582..634
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 674..726
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 766..818
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 858..910
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 950..1002
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1042..1094
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1134..1186
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1431..1664
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1712..1825
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1834..1950
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1980..2097
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1160..1187
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1359..1421
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1761
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1883
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2030
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2099 AA; 224683 MW; C0AF3F35829171CD CRC64;
MSNQTSERAR DSVAVDSLNS HDHKTMAFDD ASALLEVLVA VRRGDFSVRM RSDLTGVTGK
IADALNDIIA GNQRMAQQLE HVGQVVGRDG RTSTRVRFGL SDGSWSEMEG SINGLIDDLL
WPTTAVTRTI TAVAKGDLLQ TVPLDVDGRA LKGEFLRSAD IVNTMIKQLS VFTSEVTRVA
REVGTDGKLG GQAQVPEVTG VWKDLTESVN SMASNLTAQV RNIAEVTIAV ANGDLSKKIT
VDVRGEILQL KEAINTMVDQ LRSFASEVTR VAREVGTEGK LGGQALVPGV AGTWKDLTDS
VNAMCGNLTA QVRNIAQVTT AVARGDLSRK ITVDVSGEIL ELKETINTMV DQLNGFAGEV
TRVAREVGTE GRLGGQAQVP GVAGTWKDLT DNVNSMASNL TAQVRNIAEV STAIANGDLS
KKITVTVSGE ILELKETINT MVDQLNAFAS EVTRVAREVG TEGRLGGQAN VRGVAGTWKD
LTENVNSMGG NLTAQVRNIA EVSTAIANGD LSKKITVDVK GEILELKETI NTMVDQLNAF
ASEVTRVARE VGTEGRLGGQ ANVRGVAGTW KDLTDSVNSM ASNLTGQVRN IAEVATAVAQ
GDLSKKITVT VSGEILELKE TINTMVDQLN GFAGEVTRVA REVGTEGRLG GQANVLGVAG
TWKDLTDSVN SMAGNLTAQV RNIAEVSTAI ANGDLSKKIT VSVSGEILEL KETLNTMVDQ
LNRFASEVTR VAREVGTEGK LGGQAQVPGV AGTWKDLTEN VNSMASNLTG QVRNIAEVTT
AVARGDLSRK ITVDVKGEIL ELKNTINTMV DQLNAFAGEV TRVAREVGTE GKLGGQAQVS
GVAGTWKDLT DSVNSMAGNL TAQVRNIAEV ATAIANGDLS RKITVDVRGE ILLLKDTLNT
MVDQLRSFAG EVTRVAREVG TDGRLGGQAV VPGVAGTWKD LTDNVNLLAA NLTTQVRNIA
EVTTAVARGD LSRKITVDVK GEILELKNTI NTMVDQLNAF AGEVTRVARE VGTEGKLGGQ
AQVPGVAGTW KDLTDTVNVM AANLTEQVRG IVKVVTAVAN GDLKQNLTVA SKGEVAALAE
TINNMTNTLA TFADQVTTVA REVGVEGRLG GQANVPGTAG TWKDLTGNVN LLAANLTTQV
RAIAEVATAV TKGDLTRSIK VDARGEVAEL KDNINTMIDN LRLTTERNTE QDWLKTNLAR
FTNMLQGQRD LTLVGKLLLS ELAPLVSAHQ GVIYQVDADE EQPFLSLLSV YAQGVEAAHP
PRLDFGQGLV GQCASDARRI LVTDLPENVV PISSGVFTTL PRSAIVLPVH FEGQVKAVIE
LASAGEFTEL QLSFLDQLTT SIGIVLNSIE ATMQTEGLLK QSQKLAAELQ TQQRELQQTN
EQLGQKAQQL EERNVEVEAK NQEIEQARRA LEEKATELAL TSKYKSEFLA NMSHELRTPL
NSILILGQQL GENPDGNLSG KQVEFAKTIH GAGTDLLNLI SDILDLSKIE SGTVSVDAEE
IFVSNLLEVM ARPFRHEAEN RSLSFAVEIG GDVTKSIITD SKRLQQILKN LLSNAFKFTA
QGGVTLRVAL AASGWSPDHP SLRHAPSVIA FEVVDTGIGI PPEKQRIIFE AFQQADASTS
RKYGGTGLGL AISRELANLL GGEIQLRSTP GVGSTFVLYL PLTYVGAGAV APKSLPSANV
VEFAEAAASR RAEKTIEHVA DDRHQIAAGD SVLLVVEDDA HYARVLVDLA RDSGFKVLVA
MRGSDALSLA QDYRPAAISL DIFLPDMLGW TVLSQLKQNP QTRHIPVQII SLDEDRQHGL
TRGAFAFMSK PTTPEGLGKA LSRLKAYAQP RRKHLLLVED NEAERLSVTA LLGHDDIDIT
SVGSGSEALA ALRQDPPDCV VLDLSLPDMS GFDVLEQIRD DAEIGEVPVV VFTGRELSPE
EDATLHSMAR SVVVKGVESP ERLLDETALF LHRVVADLPL AKQATLQELH SSDEDLVGET
VLLVDDDARN IFALSSVLER RGMRVLTATT GSEAIDVINN EPSVAIVLMD IMMPGMDGYE
TMQVIRSEPR FRRLPILALT AKAMKGDREK CLEAGASDYL AKPVNTEQLL SALRMWLHR
//