ID A0A0Q4Q643_9GAMM Unreviewed; 886 AA.
AC A0A0Q4Q643;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF01_16940 {ECO:0000313|EMBL:KQN95631.1};
OS Stenotrophomonas sp. Leaf70.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1736233 {ECO:0000313|EMBL:KQN95631.1, ECO:0000313|Proteomes:UP000051583};
RN [1] {ECO:0000313|EMBL:KQN95631.1, ECO:0000313|Proteomes:UP000051583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf70 {ECO:0000313|EMBL:KQN95631.1,
RC ECO:0000313|Proteomes:UP000051583};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN95631.1, ECO:0000313|Proteomes:UP000051583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf70 {ECO:0000313|EMBL:KQN95631.1,
RC ECO:0000313|Proteomes:UP000051583};
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:KQN95631.1}.
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DR EMBL; LMLT01000010; KQN95631.1; -; Genomic_DNA.
DR RefSeq; WP_055773056.1; NZ_LMLT01000010.1.
DR AlphaFoldDB; A0A0Q4Q643; -.
DR Proteomes; UP000051583; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQN95631.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 415..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 659..876
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 886 AA; 96654 MW; 9F9237728E70AC72 CRC64;
MNDPRSRQAD ALAESLQREA GGKLTAFLGA APGVGKTYAM LTRAQEQRRR GVDVVAAVVE
THGRSDTAAL LGGLPAIALR EVDYRGHRLQ EMDLDAVLAR HPALVLVDEL AHRNAPGSRH
ERRWQDVMEL LDAGIDVWTT INIQHLETLN DVVMRITGVR VGETVPDVVF DRLHDIVLVD
LPPRELIERL RQGKVYVPEQ AAQALQAFFS PANLTALREL AMQEAADRVD SSLREARAAR
GEGNLPLRRR VLVAIDGGGQ SEYLVRVARR IAERRDAPWT VVTVRNRRHD EATGREIDAA
FALARRLGGD AELLHGPGIA DVLLDYASHN AVSTLVLGRT RERPLARLFN QTLTQQLIQR
GAHYEITIIS TPQARASARR TGLSLDPENW SRDAALALLA TAAACLAAWL GERWIGLSDL
AMVFIVAVVL VAARTRMSAA VLAATLCFLA YNFFFIAPRF TFAINARQGV ITVFLFLAAA
LVAGRLASRL RMQVVALRAA NRHANVRQAL GRQLVGATDN AQVAHAGRVA LEQALDSPAW
VRIAQDTSTS GSAAPGATDL AAADWALRHG QPAGRFTDTL AGADWWFLPL LDGEGHGIGV
AGLRLDRQYP RLAPEQRQLA EAMADDIAQA ALRTRLVADL ETAHLHNETE RLRSALLSSV
SHDLRSPLAA MIGSADSLSS YAEAMDASDR RALLDTIVVE GERLDRYIQN LLDMTRLGHD
GLKLNRDWIG VDELIGSAAR RLQRYQPDAL LKLDIPHDLP PIWVHPALVE QALFNVMENA
AKFSPPGIAV EVRARLHGGE LCIEVIDEGP GIPDAERARI FDMFYSVERG DRGRQGTGLG
LTICQGMIGA HGGHVEALPG RDGRGTLVRM TLPLLQPHPE SPRDDG
//
