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Database: UniProt
Entry: B6A1T9_RHILW
LinkDB: B6A1T9_RHILW
Original site: B6A1T9_RHILW 
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};
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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
//
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