ID C6B5G4_RHILS Unreviewed; 2099 AA.
AC C6B5G4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rleg_5109 {ECO:0000313|EMBL:ACS59322.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OG Plasmid pR132501 {ECO:0000313|EMBL:ACS59322.1,
OG ECO:0000313|Proteomes:UP000002256}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS59322.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS59322.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS59322.1,
RC ECO:0000313|Proteomes:UP000002256};
RC PLASMID=Plasmid pR132501 {ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
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 WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(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; CP001623; ACS59322.1; -; Genomic_DNA.
DR RefSeq; WP_012755467.1; NC_012848.1.
DR KEGG; rlg:Rleg_5109; -.
DR HOGENOM; CLU_000445_3_0_5; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000002256; Plasmid pR132501.
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; 11.
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:ACS59322.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:ACS59322.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
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 1355..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; 224765 MW; 108D35C5A4AEB9CD CRC64;
MSNQTSEFAR DSVAVDSLNG HDHKTMAFDD ASALLEVLVA VRRGDFSVRM RSDLTGLTGK
VADALNDIIA ANQRMAQQLE HVGQVVGRDG RTSTRVRFGL SDGSWSEMEG SINGLIDDLL
WPTTAVTRTI TAVVKGDLLR TVPLDVDGRP 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 LTLVGKMLLS ELAPLVGAHQ GVIYQVDADE RQPILSLLSV YAKGGEAAHP
ARLEFGQGLV GQCASDARRI LVTDLPDNVV PISSGVFTTL PRSAIVLPVH FEGQVKAVIE
LASVGEFTEL QLSFLDQLTT SIGIVLNSIE ATMQTEGLLK QSQQLAAELQ TQQRELQQTN
EQLGQKAQQL EERNVEVEAK NQEIEQARRA LEEKATELAL TSKYKSEFLA NMSHELRTPL
NSILILGQQL GENPDGNLSG KQVEFAKTIH GAGTDLLNLI SDILDLSKIE SGTVSVDAEE
IFVSNLLEMM ARPFRHEAEN RDLSFSVDVG ADVAKSLITD SKRLQQILKN LLSNAFKFTA
QGGVTLRVAS ATSGWSSDHP SLKHAPSVIA FEVVDTGIGI PPEKQRIIFE AFQQADASTS
RKYGGTGLGL AISRELANLL GGEIQLRSTP GIGSTFVLYL PLTYVGAGAA APKTVPSANV
VEFAEAAANR RAEKPIEHVE DDRHQIEAGD SVLLVVEDDA HYARVLVDLA RDNGFKVLVA
MRGSDALALA QDYRPAAISL DIFLPDMLGW TVLSQLKQNP QTRHIPVQII SLDEDRQHGL
TRGAFAFMSK PTTPEGLGKA LSRLKAYAQP RRKHLLLVED NEAERLSVTA LLGHDDIDIT
SVGSGSEALD ALRQNAADCV VLDLSLPDMS GFDVLEQIRD DAEIREVPVV VFTGRELSAE
EDAALHSMAR SVVVKGVESP ERLLDETALF LHRVVADLPA AKQATLQELH SSDEDLVGET
VLLVDDDARN IFALSSVLER RGMKVLTATT GSEAIDVINN EPSVAIVLMD IMMPGMDGYE
TMQVIRSEPR FRRLPIVALT AKAMKGDREK CLEAGASDYL AKPVNTEQLL SALRMWLHR
//
