ID L7U938_MYXSD Unreviewed; 762 AA.
AC L7U938;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MYSTI_02776 {ECO:0000313|EMBL:AGC44092.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC44092.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC44092.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
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; CP004025; AGC44092.1; -; Genomic_DNA.
DR RefSeq; WP_015348353.1; NC_020126.1.
DR AlphaFoldDB; L7U938; -.
DR STRING; 1278073.MYSTI_02776; -.
DR KEGG; msd:MYSTI_02776; -.
DR PATRIC; fig|1278073.3.peg.2826; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_024627_0_0_7; -.
DR OrthoDB; 5487456at2; -.
DR Proteomes; UP000011131; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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 Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 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; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGC44092.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AGC44092.1}.
FT DOMAIN 2..117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 154..201
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 257..328
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 331..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 394..622
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 643..759
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 692
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 762 AA; 83727 MW; F3F9E1101C328BF5 CRC64;
MRVLIVAQGG ADLSPLEALL EERGDTVVHV SRDVEVPAAW RAGACPLVVL DARDEGSRVP
LVRALRSLPG GNAAVVLMVA QRGALHTATL ALEEGADDIL AWPMDTEELT LRLGMAERRS
LRRESRAGVP FGDALRDTLL AVSPVPTCIT TLVEGRVVAA NDAYFRAFGY TREEMLGKTT
VELHLWDRPF DRAQVMERLR QHGAVRGVDA RYHTRTGEVR HTLLFMGLVP LGDEPHVISF
FPDITPLKQA EEELRRSEVS FRTLIQSLPD LVAVFDRDAR VRYANLKVAR ALGYSDVREL
VGKHISDMIP PEDLASADAR MHEALRTGRN ALQDRRMVRR DGGILHVEST TFPLHFDGED
SIVSVAHDLT ERHQMQARLR LAERMASVGT LAAGVAHEIN NPLAYLTANL AFAREELSHL
PAPGEPGVDP ELLRSLADAQ SALAEAQQGA ERVRTIVRDL KTFSRVDALE DSVIDVRQVL
DSTLNLATTE IRHRARVVKS FEDVPPVRAN ESRLGQVFLN LLVNAAQAIP EGAPERHEIR
VTTRLGDASR VMVEVADTGV GIATEHLPRL FDPFFTTKAP GVGTGLGLSI CHNLVTALGG
EIRVRSAPGK GSTFQVLLPA SEHPRVEPEP LVVEAPVVEK RGRLLVVDDE PLVCTALGRT
LRPHHDVTLA TRAQDALERI EAGEHYDVVF CDLMMPGMSG MDFYSTLLKR HPDQARRVVF
LTGGAVTPQA RAFLETVTSP HIEKPFAGRE LLSLVQERLA RV
//
