ID A0A0Q5I5H5_9BURK Unreviewed; 680 AA.
AC A0A0Q5I5H5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF77_01315 {ECO:0000313|EMBL:KQQ96670.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ96670.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ96670.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96670.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ96670.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96670.1,
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:KQQ96670.1}.
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DR EMBL; LMOJ01000001; KQQ96670.1; -; Genomic_DNA.
DR RefSeq; WP_056333307.1; NZ_LMOJ01000001.1.
DR AlphaFoldDB; A0A0Q5I5H5; -.
DR STRING; 1736272.ASF77_01315; -.
DR OrthoDB; 9087351at2; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051760}.
FT DOMAIN 254..309
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 320..538
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 560..676
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 609
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 680 AA; 74283 MW; 7FD397E74877CD2B CRC64;
MSDRGTAADI PDDGQEPSLR FLSGGGEVGA LMRSQDWSRS PLGEPATWPA ALRTIVSLML
GSGFPMFCAW GKDLGFLYND PYIPILGDKH PASLGAPFHD IWAEIWDDIH PLIERALGGQ
ATYMEKLPLV MHRHGYDEQT YFTFSYSPAR DDDGDVAGVH CACVEVTGQV QAERYRDEEN
QRLMTLFEQA PGIIAVVRGP DHVFEITNKS YMQLIGRTDL VGKTAREALP YVEGQGFFEL
LDQVYTSGEP FVGHAVPFDL TRGPDAPLER RYLDFIYQPI RDAAGAVVGI FVEGSDMTVR
KQVEDELRAA NRQKDQFLAM LAHELRNPLA PITTAAQLLK LGTLDAKAVR NASDIIARQA
EHMTDLVNDL LDVSRVTRGL VTLEKEELDV NAVVAGALEQ VRPLIESKRH SLTMQLSGEP
VHVLGDRTRL VQVLSNILNN AAKYTPSGGD IRLKVSAPDD DVVVCVTDNG IGVEPDVLPY
IFDLFTQAER TPDRSQGGLG IGLALVKSLA ALHGGSVEAR SEGPGKGSQF EIRLPRLSVP
EAAPDASAGD EDTVQTEPLR VMVVDDNQDA AQMLAMLLEV QGHAVSVEFD GRGALQRART
ERPQVVLLDI GLPDTDGYAL ARQLRAMSET HDATLIALTG YGQDEDRRQA EEAGFDHHLV
KPADLARVAE ILAQVPRARA
//
