ID L7TY14_MYXSD Unreviewed; 760 AA.
AC L7TY14;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MYSTI_00052 {ECO:0000313|EMBL:AGC41411.1};
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:AGC41411.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC41411.1, 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; AGC41411.1; -; Genomic_DNA.
DR AlphaFoldDB; L7TY14; -.
DR STRING; 1278073.MYSTI_00052; -.
DR KEGG; msd:MYSTI_00052; -.
DR PATRIC; fig|1278073.3.peg.57; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_44_7; -.
DR OrthoDB; 5525648at2; -.
DR Proteomes; UP000011131; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGC41411.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AGC41411.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 184..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 220..273
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 295..347
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 528..744
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 760 AA; 83778 MW; C04FBA4D22DD342B CRC64;
MGRRWTFSQR VGAGFIASLL VALALAVTSA VALLSVRTHQ KASLLELSMD LLEVERLRRA
FSDKVSSERG YALSGDTLFA EEMVASRERF ISIAGRLEAR LVVEPASSLL GSAMRAEQEH
EQAVRELVVA HAANVPRSKL ERLFEERVGT TRLRAYESLQ QLSANAEEQL ARGIQTAVDV
DERVLGLTLV AASLGLAVAA VLAWVLLRRL RPLREEADDS ARRFQLLVEG VQDYALLLLD
ARGRVASWNP GATRITGYEA SEVVGEPVDL FYPPESAALG VPEKDLARAR RDGRLRTEGW
RRRKDGSSFF AEALINVLRD ESGALRGYAE VTRDITERRR AERTQGLFAE AGRVFQQYPE
PDLMVAELSR MMVPEVADGC VLYVLTPSGQ LRPRVVKHAD EEKEPLLWEA VRRHQPSPDT
PRGLWQVMRT GRSHRVADVT PEMLAKNAED AEHLRMMEQV GVRSYLAVPL RSGEKAQGVL
VLLTSSPERR LTQGDQVFME ELAGRAALAL DNTRLLRESR EAVELIGIAA HDLGNPLNTL
QLLLRKLQRQ GPGMAPEKLR DGLAAALKQT QRLGQLLLNL LDLSRLSAGR LVLDVATVDL
ADLAHEVVER FAAYASEQGS KLVFDAELGL VGGWDRLRLD RVVTNLLSNA LKFGAGQPVE
VRVERAGLSR ARLVVKDHGV GIPPEAQRRI FDRFEQVPSE GRHAGFGLGL YIVRQLVDAH
GGSVHVESSP GEGSTFTVEL PLLQQGSERE LPGTEPPVLP
//
