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Database: UniProt
Entry: Q1DFI9_MYXXD
LinkDB: Q1DFI9_MYXXD
Original site: Q1DFI9_MYXXD 
ID   Q1DFI9_MYXXD            Unreviewed;       714 AA.
AC   Q1DFI9;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=MXAN_0304 {ECO:0000313|EMBL:ABF86169.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86169.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF86169.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF86169.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1DFI9; -.
DR   STRING; 246197.MXAN_0304; -.
DR   EnsemblBacteria; ABF86169; ABF86169; MXAN_0304.
DR   KEGG; mxa:MXAN_0304; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_44_7; -.
DR   OrthoDB; 5482955at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 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; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABF86169.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transferase {ECO:0000313|EMBL:ABF86169.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        35..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          485..705
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          125..152
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   714 AA;  78416 MW;  5F49CF6028DA2AAE CRC64;
     MRGSSPAVCM QPAGSPPLTM HARPERHHPL WASRAGRYGV ALLAFVAAWL IQAGTMSFIP
     ATPFLFFFGA VMVSGWWGGW GPALATTLLS VVVVDFYFLE PLLNLMPGTG GAVSLAVFVV
     LALLMTKLNV MLRKANAERA RLLERERAAR SEAEAGQARL HALFRDAPAA IILMHGPRHI
     YSFSNTMNNT LMGTDTLVGQ EASKALPWAE SRGFITLLDE VYRTGVPFTG NAVPFPRKPP
     HDEIQETYLN IVYQPTRNEQ GEVDGIAGFG FDVTDLVRAR QRAEALTHEL QLAEARDWLL
     AESGAVLASS LDDETTLRNM AKLVVPTFAD WCLVDVAEPD GTFRRLEAAH FRLEDDALAE
     DILRFGMQPS GNPGHPPTGA LLKAETVHVE RLTRERIHEL AHDAEHARVL EAIGPVSFIA
     VPLIARGQVL GVLSFIHAHS GRHYSTSDLA FAKELAHRAA LSLENARLYA EAREAIRLRD
     EFMSIASHEL KTPLTPLSLK LQALSRELAR HPGPVPRNLV ESYVAVGARQ VQKLAELVGD
     LLDVSRISAG RLSLELEELE LGSLVRDVVT RYEPQAARTG SPLQLEAGDF DIVGRWDRLR
     LEQVITNLVD NAVKYGNGRP IHVRLEPHDG GARLTVRDEG IGIEPQHLPR LFGRFERAVS
     ERNYGGLGLG LYITRTLVEA MGGRVHVESR LGRGSTFTVE LPSHLGAEQA RQAP
//
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