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Database: UniProt
Entry: L7U748_MYXSD
LinkDB: L7U748_MYXSD
Original site: L7U748_MYXSD 
ID   L7U748_MYXSD            Unreviewed;       497 AA.
AC   L7U748;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=MYSTI_00965 {ECO:0000313|EMBL:AGC42314.1};
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:AGC42314.1, ECO:0000313|Proteomes:UP000011131};
RN   [1] {ECO:0000313|EMBL:AGC42314.1, 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; AGC42314.1; -; Genomic_DNA.
DR   RefSeq; WP_015346577.1; NC_020126.1.
DR   AlphaFoldDB; L7U748; -.
DR   STRING; 1278073.MYSTI_00965; -.
DR   KEGG; msd:MYSTI_00965; -.
DR   PATRIC; fig|1278073.3.peg.1006; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_89_29_7; -.
DR   OrthoDB; 9781147at2; -.
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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGC42314.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          184..239
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          270..490
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   497 AA;  53664 MW;  33DD799846ACDFE0 CRC64;
     MRLARKFTLA LVLLAVAVIA GLQVIQVRRE LERSALDMQH DHRLLGHALA GTISKAWELA
     GEREALNLLH QSNNFQEQVH LRWVWLDGGP GTPSLVGFPP RLLATLRQGK DGSMVDPEPA
     PGLLHSYTPV FIGLGVGRRF GAIEITESLG EERQHVFVTV VGTIVATGTI TFAFFIVAMA
     MGRRLVGEPV DQLVQLAHSF GQGDLTARVR LPPKRRGDEL TTLANAMNRM GEQLEETRSR
     LSTETTARLA AVEHLRHADR LTTVGKLASG VAHELGTPLN VVMGRSKMIS SGEAEGEEVA
     ECARIITQQT QHMTGIIRQL LDFARRRAPH RAPEEVRELV ARSLSLLKPM ASKKSITLVE
     DVPPDVMLEA DGGQVQQVLT NLVMNALQAM SKPGTVSVRA ALIRATPPQD VGGAEGSYVR
     VDVEDEGPGI APDVLGHVFE PFFTTKDVGE GTGLGLSVSY GLVRDHGGWI AVRSELGRGS
     CFSIYLPSGG DTCQAAS
//
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