ID V9XEV4_9NOCA Unreviewed; 491 AA.
AC V9XEV4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Y013_07490 {ECO:0000313|EMBL:AHD20520.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD20520.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD20520.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD20520.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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};
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DR EMBL; CP006996; AHD20520.1; -; Genomic_DNA.
DR RefSeq; WP_006550235.1; NC_023150.1.
DR AlphaFoldDB; V9XEV4; -.
DR GeneID; 29938587; -.
DR KEGG; rpy:Y013_07490; -.
DR PATRIC; fig|1435356.3.peg.1496; -.
DR eggNOG; COG3920; Bacteria.
DR HOGENOM; CLU_045351_1_0_11; -.
DR Proteomes; UP000018781; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.280; GAF domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR038424; H_kinase_PdtaS_GAF_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR022066; PdtaS_GAF.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12282; PdtaS_GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 293..487
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 52807 MW; FFB845975524E1B7 CRC64;
MSTLSSLLAR YTDLPGAAVD HLQRVVGEWQ LLADLSFADV LLWVDAAPSG IVCVAQCRPT
TASTVIPEDA VGTLVSDNEH PYVRKAFETG EIVDVKSSPG AGINIRQAVP VRWDGRVVAV
LSRDAARVSR RSASALETAY LECADDLYRM ISEGTFPTPE ARSDTKSSPR AGDGFIRLDR
KGKVVYASPN ALSAYHRMGL NSDLIGQDLV ETTRALVTDP FESRDVTDYL RGAVEGRLGQ
RMEIEALGAT VLIRALVLNP GGKIRGAAVI VRDVTEVKRR DRALLSKDAT IREIHHRVKN
NLQTVAALLR LQARRTGNAE AQQALGEAVR RVTSIALVHE ALSMSVDEEV DLDGVFDQLI
PIVVDVSTVG SQIRVVREGN LGVFPADRAT PLVMVLTELV QNAVEHAFDP GVNGTVTVNA
QRSARMLDVV VRDEGKGLPE GFSLEASNRL GLQIVRTLVA AELGGSLELT SNEVGGTDAR
LQLPLGKVPV A
//
