ID A0A0Q6LKF3_9BURK Unreviewed; 938 AA.
AC A0A0Q6LKF3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC88_12015 {ECO:0000313|EMBL:KQU64421.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU64421.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU64421.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU64421.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU64421.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU64421.1,
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 -!- 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:KQU64421.1}.
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DR EMBL; LMCN01000045; KQU64421.1; -; Genomic_DNA.
DR RefSeq; WP_056807855.1; NZ_LMCN01000045.1.
DR AlphaFoldDB; A0A0Q6LKF3; -.
DR STRING; 1736511.ASC88_12015; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000051195; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd17574; REC_OmpR; 2.
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 InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 691..804
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 813..930
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 149..179
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 740
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 862
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 938 AA; 102378 MW; 0D7918D43B47A81A CRC64;
MTRLSVQQLA TAGFLVAVAA ILSLAGIGWN FARQTLEASG FVSRTHQVIS VTSDIQSDIY
RSEAAQRAYI ASRNPVYLDE RDATLAVIDT GLRQFSWLTA DNPQQQARAA ELRGEIAARV
QVFHENESLQ PNETPQALDE RLSRGVRRLE RVRALLDQIN TEERRLLAER ERVEDQRSQS
TVTTFIVFLV ALVLLLGAIA WRLRLDWAAR QRAEQAVGEE RRYDALHARA LTLYNAQATR
EVVLAETLAL IGENPLFPVA VFYEHEEWGG VLRTVARHNA PADLKGVLRI DDGLVGAVAR
SGKPAYLEHF DAASGLRIET GLASLRPAAL LICPVSYQGR LIGVLALAAA APLSTRDRGF
IERLCAQFAV ALHNLGQLQE LNLLAEQLRV RGEDIQVKNA ELEKADRMKS EFLANMSHEL
RTPLNAVIGF SGLMKDGLAG DLNAEQREYA NDIHVSGKHL LSLINDILDL SKVESGHMPL
ELGAAEPSHI MTSAASLMRE KAATRRLRLN AVCAPDLGSL QLDLRKSKQI VFNLLSNAIK
FTPEGGVVTL AMKRVARADV DGVLEAQDTR VFRPSERTLP SFLEIRVEDS GIGIAPDGIG
RLFQPFVQID SSLSREYEGT GLGLTMVKRL VELHGGGLML RSTPHVGTTF VVWLPWRPAG
DETQREPPLP EPVGLPAAHG RLREAGPDAP LILVVEDDPR TATLMRAQLE SDGYRVEVAR
SAEEGLTRAA ALMPAALVLD IILPGRDGWD LLSQLKEQPQ TGHIPVVIVS ITAEARRGFA
LGASQVLTKP VSKDDLLAAL AAVGLDGKLP AARVLVVDDD PKAVTLVGKH LQSAGLVPML
AYSGREALEV VHQQRPALIV LDLMMPQLSG FDVIEALRGR SDTADIPIIV LTAKLLTVQD
RALLSGRVQQ VMEKSDFQPA SLLAEVRRAL AKGRPRQA
//
