ID A0A0Q7SSE5_9BURK Unreviewed; 837 AA.
AC A0A0Q7SSE5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASD35_02445 {ECO:0000313|EMBL:KQY90684.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY90684.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY90684.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY90684.1,
RC ECO:0000313|Proteomes:UP000051648};
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:KQY90684.1}.
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DR EMBL; LMFP01000001; KQY90684.1; -; Genomic_DNA.
DR RefSeq; WP_056873302.1; NZ_LMFP01000001.1.
DR AlphaFoldDB; A0A0Q7SSE5; -.
DR STRING; 1736464.ASD35_02445; -.
DR OrthoDB; 8579121at2; -.
DR Proteomes; UP000051648; 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; cd00130; PAS; 2.
DR CDD; cd12915; PDC2_DGC_like; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..385
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 416..467
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 473..523
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 541..593
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 611..828
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 837 AA; 88801 MW; 00BE368F26BAC821 CRC64;
MQPRGSRWRP SIIVAGAGVL LAAVLLVGAG YGLWREQSKL TAETAERQAL LARVLEDHAS
RSLDATQIAL AGLADVAARG APPEVLQALL GQTQASLGFL RGVALLDEGG HVLAAADPAD
RGVQLAPAAL GPWPAPGRDA VGGFVAARSL AGLAGTGEAS VVPPGVGFIP VLRGLRLPDG
RGALLTALLN PDALANFQQL TLNDPQAAAA LVDLDGRLLA ATHGAGQLAG ERLARLLAAG
APLARVRAGS EHGRWEGAGL REEAQLGSYR ALRARPLVVL VELPQAELRS HWLATLRDLG
LPAFGVAAAL LTLSGIGAAA LRGRERAALE LDRAQREVAE REGELSAIFG SVQDLLFRTD
AAGRVTFINE GYARLSGHAA GRVVGLPLQQ LFGGSPRVAA LFDARDADEA DEAQPHQVRA
DWLAPDGQAR SFEIHLVPLR RSDGVLEWVG SAADVSGLMR AQAELRAQLG LARSLLASSP
LPMSVLDSDN RYLDVNRAWE QFTGRKRGDV LGRRAAGYLR PEEAALHDAR DAELLARGGE
MNYEAVWHGA DGRRRDLFIS KATFPDAQGR PMGIVVCFMD ISEFREAERA TRAARDAALQ
ASRAKSDFIA NVSHELRTPL QSILGFSEIG ALRTRQEPRL AELFADVHRA GERMLSLVND
LLDLSKIEHG AEPIQPERLD LRPLATEVAR ELRPQLAAKG LQLQTALADE ELVVLADPLR
LLQVLRNLLA NAIRFSPEGA SIELTAVHDE AGEVRVDVAD RGPGIPPAEL ETIFEAFVQS
SATREAAGGT GLGLAICRRI AQAHGGRIWA ANRDGGGAVI SLVLPATRFG DTTRAAL
//
