ID L7U6G2_MYXSD Unreviewed; 980 AA.
AC L7U6G2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MYSTI_00709 {ECO:0000313|EMBL:AGC42059.1};
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:AGC42059.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC42059.1, 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; AGC42059.1; -; Genomic_DNA.
DR RefSeq; WP_015346322.1; NC_020126.1.
DR AlphaFoldDB; L7U6G2; -.
DR STRING; 1278073.MYSTI_00709; -.
DR KEGG; msd:MYSTI_00709; -.
DR PATRIC; fig|1278073.3.peg.737; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_25_7; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000011131; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 4.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 4.
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; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AGC42059.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AGC42059.1}.
FT DOMAIN 217..273
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 357..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 607..720
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 732..846
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 860..975
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 264..353
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 656
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 781
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 908
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 980 AA; 106888 MW; BFD2B35910924DC5 CRC64;
MVNTLSPLVP PTDTATLLVV GSERECQRVE EALGHAGVTA SAERATTLPA LEAALARSWS
LVVCGSEVPG LGFAEAQGLW RKQQRELPFV VLSREWSDDT LEASTRAGAR DYVSEDHFNR
LAPVLRRELP LAGAQLRHDA TTEELLRTNW ILGNILDALP FVLFVKDAKT RRLVVVNKTF
ADAFNVTKEW LLGKLDHDYF PPEQADSFIT IDSEILASKK MRAFEEVARA GGVDRIFATR
KLPLMDGSGD ASYLLGVTED ITERKQNEEM LRASKAELEA ANKQLAASLE EIKRTRAVSA
RSLASYQQRA LQMEIIRQQN EDLDRLAQEL AVAKRNEEER AREAEAAARL KSEFLANFSH
EIRTPLNGII GYCDLLMREE GSRLTAHGRR DLNVVKTNAK TLLALINDIL DLSKIEAGRV
EVVSEAVDVR ELADECMATV KEYLKGKDVA LTTHIDVAAG ILRTDALKLR QIMLNLLSNA
AKFTETGEVA LSVVPAGEEV VMTVEDTGVG IPSDQLPFIF EKFRQVDGST TRKVGGTGLG
LAIVRELSRV LGGNVTVTST LGRGTTFTVR LPNMTDAPSD GPTSVERAVP VAEVAHHLHA
VAQPGSTVLV VDDDPLIQQL VTGQLAPAGF KVVVAEDGIA ALKRARELKP QAILLDIHLP
KLDGWSVLSQ LKSEPALAGI PVILISVEEQ RARGFSLGAC EYLVKPVEPE RLVEVVQRCL
GPTNGTAAGV GEVLVVDDDA ATRELVSRNL RRAGFSTAEA RNGEDALLKA RVSPPSLVVL
DLMMPNLDGF EVLRRLRAEK LQVPVVVLTG KSLTSDEEAL LRDGFAGFVK KGGHALEDVI
AQAKGLLLSQ RAATAGRLPR ILYVEDSAQN RDIVRRYLGG LFEVIEAEDG EHGLERATRD
NPDLILMDLS LPRLDGWEAT RRLRAVPSVA NVPVIAVTAH AGREYQDKAH AAGCTAYLTK
PLDRDQLLEM IRKHLGRSHG
//
