ID A0A225DT68_9BACT Unreviewed; 499 AA.
AC A0A225DT68;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FRUB_02453 {ECO:0000313|EMBL:OWK44521.1};
OS Fimbriiglobus ruber.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Fimbriiglobus.
OX NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK44521.1, ECO:0000313|Proteomes:UP000214646};
RN [1] {ECO:0000313|Proteomes:UP000214646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA Mardanov A.V., Dedysh S.N.;
RT "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT Planctomycetales with confirmed chitinolytic capability.";
RL Submitted (JUN-2017) 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:OWK44521.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIDE01000003; OWK44521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225DT68; -.
DR OrthoDB; 3272385at2; -.
DR Proteomes; UP000214646; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:OWK44521.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000214646};
KW Transferase {ECO:0000313|EMBL:OWK44521.1}.
FT DOMAIN 19..63
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 134..352
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 373..489
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 422
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 499 AA; 53894 MW; 55FC63CA842643E7 CRC64;
MSDAPDAARE RYEHALRASE SRFRDVIEKN ADGIVVMSRD GVVRYVNRAA EQLFGYPASA
FVGTLFGVPI VPDGRTEVDL HGSAAGGVAE MRVVETEWEG EPAFLASLRD VTDRKRAEEA
VKEADRRKGE FLAMLAHELR NPLAGISNAL HVLGIPGVNS GHTERARGVA ERQIQHLTRL
VDDLLDVSRV THGKIRLKKE PVDVVAAAAR AAETVAPAIE AHEHEFLLSL PDEPVWVEAD
ATRLEQILAN LLNNAAKYTL PGGRIWLSVM DQGDEVAISV RDTGVGIPPD VLPHVFELFA
QAGRTLDRAQ GGLGIGLTLV KNLVEMHGGS VSADSGGAGR GSEFVVRLPT VPGRKPDDTY
RADPGHPAER VCRVLLVEDQ KDAAEMLAEL IRMWGHQVVV AHDGPAAVAI AEAHCPEVIL
LDIGLPGMNG YEVATRLRGH PGMKGAKLVA LTGYGQEEDR RRSKQAGFDQ HLVKPVAPRE
LERILAETGR SRADGDGRG
//
