ID A0A0Q7CNI4_9CAUL Unreviewed; 461 AA.
AC A0A0Q7CNI4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC73_18570 {ECO:0000313|EMBL:KQW66390.1};
OS Phenylobacterium sp. Root1277.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW66390.1, ECO:0000313|Proteomes:UP000051150};
RN [1] {ECO:0000313|EMBL:KQW66390.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW66390.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW66390.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW66390.1,
RC ECO:0000313|Proteomes:UP000051150};
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:KQW66390.1}.
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DR EMBL; LMDZ01000009; KQW66390.1; -; Genomic_DNA.
DR RefSeq; WP_056026275.1; NZ_LMDZ01000009.1.
DR AlphaFoldDB; A0A0Q7CNI4; -.
DR Proteomes; UP000051150; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR036890; HATPase_C_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; IPR013655; PAS_fold_3.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF07536; HWE_HK; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00086; PAC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 144..215
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 220..274
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
SQ SEQUENCE 461 AA; 49255 MW; D11F3EDBF27A756E CRC64;
MADDEQKGGW PSASAGGEAL LKAMLEASAM LAGVIEVLDD DYRFVMANRG ACEFYGCADG
GLNGRTGREL GIKAEQILGR VNVLRRVLST GAAETIEYSF RFPSGRQGWF LGTFSPLTGN
AGQVAFIIID ITQQHAAQVE AERQGARLTL ALNATELGLW EYDVAADRVD WDSRTRRMFG
LPPEGDINYA TYAAAVHIED FPATRVAYEA ALAGENDGHY VVEHRTTSGG EGGSATWVRG
AARVSFDGQG RPIHVIGTSQ DISAQVAARQ RQDLLLGELN HRVKNNLAAV QAIASQTMRN
APDDPAAFRA AFDSRIQSMA RGHDLLTRNV WEAADLRDVI DAALAPFAAE GFDIQGVEAP
APLGPEMAVN LVMVLNELAT NAAKYGALSG AGRVAIVWGV GGGNLTLHWR EYGGPPVSPP
QRSGFGTRLT RSALQAYGGS VELTFPPEGA ECRMSTPLAR R
//
