ID A0A0Q5HU84_9BURK Unreviewed; 1345 AA.
AC A0A0Q5HU84;
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:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF77_05375 {ECO:0000313|EMBL:KQQ97379.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ97379.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ97379.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ97379.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ97379.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ97379.1,
RC ECO:0000313|Proteomes:UP000051760};
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 -!- 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:KQQ97379.1}.
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DR EMBL; LMOJ01000001; KQQ97379.1; -; Genomic_DNA.
DR RefSeq; WP_056335493.1; NZ_LMOJ01000001.1.
DR STRING; 1736272.ASF77_05375; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 153..200
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 291..363
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 723..767
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 912..965
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 983..1201
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1225..1341
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1196..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1274
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1345 AA; 142861 MW; A1606DF4CC2A96DF CRC64;
MSAAVQPRIL LVDDQPANLA VLEALLAGLD AALVPVDSGE AALRALLADE FALVLLDVQM
PTMDGFQTAE LMRQHPRSQA VPVIFITAGD ADDFPYERAY ALGSADYLAK PLNAQVLRAR
VSQCLVVYRQ NAELARLRAA QSPAPAPAPA PGQSDRLRLI LDNLHGYAFI GTDTERRITE
WEAGAEEVTG WSAAEALGRS ADMIFTQEDR AAGKPDEEAA RARDTGRSTD KRWYLRKDGG
RFFADGMMIA LREEGERRGR LLGYAKIMRD ATAEHEAIEH LAASERALHE STERFARLLE
SSGEGIVGLD LDGRCTFLNA AGAACLGYAP QELAGAAAAV LLPEPAEAEG LGASALLDAV
RSGATLRLDD ARLLRKDGTR LPVACSLHPM TTGGGAGGAV LTFTDISARQ RAGLERERLV
AQLRTANERM RDIFYQAPAF MAVLRKPEMV FDMVNERFAE LVGRRALLGK SVHAALPELE
GQGLFELLDG VYRSGVAHEG SNVRLQLQTA GGELATSYVD FIYMALREPD GAVSGVLIHG
IDVTDRTRAN LLAVGQRGAL ELAVSDAPLD DVLDLLARSA EDYAGGAALA AIQLAGPGGA
LVHAAAPSLP ADLRQALDAV GIAPLGAGGG TAAWRGEPVD CPDIAGDPLW ERCRAEALAA
GLAACRALPI LAPSGAVLGA FTWYDRAGYR ADRAGADAAL ALLANTASLV IGQRAEASAR
QAAEERSHAI LESMNDGFLA LDSGWRIGYA NGAAERITGM SRDQLFGDVF WDLFPDWQGS
TQERACRRCA ADRSAQRLEV QVPAWGGWYE INCFPTPDGG IALYLRDESE RRVAEEGVRR
LAAVAEQSSD FIGIFAPDGA GLYLNPAGRA MAGLGLASDI RGARLLDFFS SDCRPFVRSD
VLPALTGAAE KWDGELKFSG RGAGDAIPVY FKGFAVHGAD GAHLGLATIT RDITEQKRAE
DELRRIAADL SQADHRKSEF LATLAHELRN PLAPIRTGLD LLRMAPPSAE TAARVHAMMD
RQLGQLIHLV DDLLDIARIT RGRIELKKEA IDLRVAVSMA VESSTALIQA GGHKLEVALP
DEPLPLDADL TRLVQVLSNL LNNAAKYTPG GGRIALAAWR EGMQAVVAVT DSGIGIAPDA
IGSVFEMFTQ VGSSLDRAQG GLGIGLSLVR RLVELHGGRV QASSAGRGQG STFTVRLPLR
RRAGDGESGE TRAAPAMPAQ ARRLRVLVVD DNLDAAESLV ALLGALGHET RMAHDGPAGL
AAARSFRPEL AFLDIGLPGM NGHEVARALR SSSELRGAVL VALTGWGAAS DMTLSQQAGF
DQHLTKPVSR EALEQALATA MEGRA
//
