ID A0A0Q5Z747_9BURK Unreviewed; 898 AA.
AC A0A0Q5Z747;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG30_18930 {ECO:0000313|EMBL:KQT13504.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT13504.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT13504.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13504.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT13504.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13504.1,
RC ECO:0000313|Proteomes:UP000051173};
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:KQT13504.1}.
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DR EMBL; LMQL01000003; KQT13504.1; -; Genomic_DNA.
DR RefSeq; WP_055892495.1; NZ_LMQL01000003.1.
DR AlphaFoldDB; A0A0Q5Z747; -.
DR STRING; 1736365.ASG30_18930; -.
DR OrthoDB; 8552871at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF08447; PAS_3; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
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:UP000051173}.
FT DOMAIN 85..137
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 204..256
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 477..528
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 539..757
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 777..893
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 826
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 898 AA; 99974 MW; ADD7DFBFAA0CA239 CRC64;
MSNDRHTPPQ ELERMDAAVR TSGVGVWLNP LPLGDLVWND NTKAHFHLPP NARPTIELFY
ERLHEEDRER VREGVERSVQ NGQLFDEVYR TVAPDGGHKW IHAVGRASVD ADGRPLRFDG
ITLDITEQVT AQQRLREFAD TAPAMLWVTE PDGVCSFLSR GWTLFTGQPE TAGLGFGWLE
MVHPRERPAA AAAFRDANSR QVDFAVEHRL RRPDGSWRWV IDAGRPRYAP DGEFLGFVGS
VTDIHDRRLA EDALRRSGNR YRRLLDSIDQ GFCVAEILLD EQGRPRDYRF IETNEVFERQ
TGLHNPLGRT ARELVPQLED FWVQVYGEVA LTGQSHRFSQ GSHAMGRWFD VFATPIGEPH
EHHVAILFQD VSHRVESEQR MRESRERYRA FVANSTEGIW RMEFDPPVET SATVQEQVQA
VLRSGRFAEC NEVFARMYGL DSPADVIGHG LELAMDPADP RVQAYLHALV ESGYRANDVE
SAERDREGRP LWFANSLSGV IEGGRLVRAW GTQRDITDRK RVEAALMEAD RRKDEFLATL
AHELRNPLAP IRSSAELMRL TAPHDDLLQR HTDIIGRQVE HLARMIDDLM DVSRISRGRL
ELRLAPVDLR DVVHAAVENA QTELQAGGHP LALDLPEEPL HLQGDDVRLV QVVLNLLTNA
VRYSAPGRPI GLSVRREDGQ AVLSVRDQGL GIAADQLPRV FELFYQGGAS PERAGGGLGI
GLSLVQRLAQ LHGGSVEARS AGLGEGSEFV VRLPLSTGTA PTVVNAAPRP APPQRRRVLI
VDDNRDAADT LAEVMEMLGY QVDTAYDGVE GLSRAEALRP QVAVLDLGMP RLDGFGTCRA
LRETEWGQAM AVVALSGWGQ AADVERATQA GFDAHMVKPV SPDALAETIE RLLSGSAR
//
