ID D0LWK3_HALO1 Unreviewed; 593 AA.
AC D0LWK3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Hoch_5165 {ECO:0000313|EMBL:ACY17653.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17653.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY17653.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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 ---------------------------------------------------------------------------
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; CP001804; ACY17653.1; -; Genomic_DNA.
DR RefSeq; WP_012830245.1; NC_013440.1.
DR AlphaFoldDB; D0LWK3; -.
DR STRING; 502025.Hoch_5165; -.
DR KEGG; hoh:Hoch_5165; -.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG3279; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_7; -.
DR OrthoDB; 9813024at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACY17653.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Transferase {ECO:0000313|EMBL:ACY17653.1}.
FT DOMAIN 10..156
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 219..446
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 472..586
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 169..210
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 87
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 519
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 593 AA; 66059 MW; F3DF8F7471EDB527 CRC64;
MRPRAQTARR ILLVDDNPSI HDDFRKILDE DLAPALDALA DILLGESVPG GQRQRFVLDS
AFQGDEALRL VEKAKDGEHP YAVAFIDLRM PPGWDGLETL LRIWEVDSRI EAVLCTAYAD
YSWEQFLERV GDSDQLLILK KPFDIAEVRQ LVHALTAKWQ LARDNERRLE RLEINLLGRT
RELASANEAL QREMNERERT ERALRKAQRL EALGRLATGI GHEINDPLTF LTTGIESISA
EFGDIRRYLP GDVHAELAEL LEAASIGVDR ISQIVRSIQL FGEKDAPDST SLEIVDLVAV
LKLSVRMVTR SLDTDIEFCT ELDEVPAVRG RRVPLEQVFV NLLNNAVQAL NSDERAGVQP
RIVVRCSSVA SGEQVRVAIA DNGIGIPAEH LEQIFDPFFT TKPVNQGTGL GLSICHSIVR
ELGGEIDVQS TEDVGTTVNV VLPVAQRDAA DDTTRDEPAL DASPEVTPRR GRILVVDDEP
LILRMMMHAL REHDVVAVTS ARDALERLRG GHFDMVLCDL MMPGMTGMAL YTELCAQQPR
LADRMAFMTG GTLLPEVQQF LADTPIECLE KPIRIQRLRS FVAERVNRSL AAC
//
