ID A0A0Q6LKC0_9BURK Unreviewed; 1409 AA.
AC A0A0Q6LKC0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASC88_10225 {ECO:0000313|EMBL:KQU65958.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU65958.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU65958.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU65958.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU65958.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU65958.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQU65958.1}.
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DR EMBL; LMCN01000043; KQU65958.1; -; Genomic_DNA.
DR RefSeq; WP_056820583.1; NZ_LMCN01000043.1.
DR STRING; 1736511.ASC88_10225; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000051195; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..213
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 236..487
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 834..888
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 889..936
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 963..1016
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1048..1265
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1290..1406
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 699..761
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1014..1043
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 63
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1339
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1409 AA; 154727 MW; 9124625E602D52B4 CRC64;
MQDLGPDHAE EEAGTELSDG IAPGDDRLPV IGLGGSAGGI PALTAFFRTV PPNPGAAFVV
ILHLSPEHES TLAELLQRHT SLRVVQVRET VQIEADTVYV IAPRNALRMV DETLQPGKLP
VERSGSIAVD LFFRTLADTH GPQAVAVVLS GADSDGAIGI KRIKERGGLA IAQDPDEAEH
PGMPLAAIAT GMVDWVLPVA DIAQRVLDYA RLASQLHLPP EQGEAALPNA PNLNGEAELR
DVLSFLRTRT GRDFSNYKRA TILRRIARRM MVNGVHELAD YMRCLRTLPG EAGALLQDLL
ISVTNFFRDA DCFTALEMHI PHLFQHKTPN DSVRVWVAAC ATGEEAYSIA ILLAEQARRL
SSPPAIQIFA TDLDEEAIRV ARDGVYPLSI SADVSEERLR TFFTKEHRGY RVRRELREMV
LFAAHDLLKD SPFSRLSLMS CRNLLIYLNR EAQHRVFETA HFALLPEGRL FLGASETVED
DSPYFFTLDK KHRIHAPRPV SRATMPVPSG AGTIARALEL QSAARGGPVI PTGGAFPREP
HVERPPADAN GRSISWAELH FKMIEMLAAP SILIDAQHEI VHLSDSAGRL LQFAGGEPSR
NLLRAIHPAL RVELRAALYK AALGNERSTV PALTVDLDGV EVAVRIGVQP MTQVVPGMML
VLLDTVPLDE IVEPAQRPPV PVEPDPLSHH LDRELVRLKA HLRDTVEQYE ASTEELKASN
EELQAMNEEL RSASEELETS REELQSINEE LTTVNHELKA KVDELGHANS DMQNLMDATA
IATVFLDRDL RITRYTPSAV ELFNLIPTDV GRPLAHLTNH LNYPTLDTDA RRVLQGLIPI
EREVDDTRQH WYLVRMLPYR TLDDRIAGIV LTLVDVTERK RGETALSATE ERLRLVVDSA
VEYAIFSMDL QRRVTSWNAG AQRLLGFSEE EILGQSCDVI FTEEDRATGA PEHEAATALS
EGRARDERTH QRKDGERFWA SGVMTPMHDE AGNAIGLVKV LRDQTAERAS TDALAQGRME
LLQALEEKEK ARLELEAADA AKDRFLAVLS HELRNPLASI AGASETLAVA PPRGDPQSRA
IRILRQQVGS MRDLLDDLLD LSRLRLGRFA MSQRRVALRG IVDAAVETAH SEIENRRHAL
TVELPARPVV LNADPSRLSQ VLSNLLINAA KYTEDGGRIA LVARTDGTEL VLTVTDNGRG
LDEKATVSMF DMFWQSEVQT RSAHSMGIGL SLVRSIVQMH GGTVTARSAG PGHGSEFTVR
LPLAPTGDDI AVDEDISPLY DEGEVTVPRR VVIADDNEDA PWSLATLLQT DGHDVASAAN
GADALALITE QRPDVALLDI AMPGLDGFEV ARRVRGEDWG RTMLLIASTG WGGESDRQAS
SAAGFDAHLV KPIDIGRLKE LIARWRPAE
//
