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Database: UniProt
Entry: A0A1M6DFL1_MALRU
LinkDB: A0A1M6DFL1_MALRU
Original site: A0A1M6DFL1_MALRU 
ID   A0A1M6DFL1_MALRU        Unreviewed;       705 AA.
AC   A0A1M6DFL1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02745165_00666 {ECO:0000313|EMBL:SHI72124.1};
OS   Malonomonas rubra DSM 5091.
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Geopsychrobacteraceae; Malonomonas.
OX   NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHI72124.1, ECO:0000313|Proteomes:UP000184171};
RN   [1] {ECO:0000313|EMBL:SHI72124.1, ECO:0000313|Proteomes:UP000184171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5091 {ECO:0000313|EMBL:SHI72124.1,
RC   ECO:0000313|Proteomes:UP000184171};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQZT01000002; SHI72124.1; -; Genomic_DNA.
DR   RefSeq; WP_072905561.1; NZ_FQZT01000002.1.
DR   AlphaFoldDB; A0A1M6DFL1; -.
DR   STRING; 1122189.SAMN02745165_00666; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000184171; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00731; CheA_reg; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SHI72124.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184171};
KW   Transferase {ECO:0000313|EMBL:SHI72124.1}.
FT   DOMAIN          1..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          363..563
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          565..698
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          245..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   705 AA;  76330 MW;  C42E0E9E9A9732D8 CRC64;
     MADQAIDDFL AESEELLDKL NQDLAKLGDG IADGGSSPDL LNGIFRDAHS IKGLAGMFGF
     NDVSELAHHL ENLLDHLRMG KVALSEALLD CLFDTLEGVS GLIRGKADSP DYTQDLTPYL
     DRIEHLLTGP VTADEGSLNI DQSLLDVLTE YEEHRLQENI SQGKTIYLVK VAFSLMTFDT
     ELTDVTEKIK SLGEVISTLP GTENDDPEML AFRILCGVSV DQQDLTGKLG RDDVAIEVLL
     GEAGGAAASQ PVAEPEPVAP PPKIEPQPKV SEPPSFIEDP MAEPAIDAQP QEEPETVPQQ
     NGESSSAKSF TSTVRVDIGK LDYLMTIVGE LALAKGSIAQ LCSEVHSAGL PIARELDKAV
     HALERRLNEL QLGVMDVRMV PVRQLFDKMN RIIRRMAQDL GKKVRLEVRG GDTELDKLIV
     EELADPLMHI IRNALDHGIE AADERLIAGK AETGTVSLIA SQRGNHVVIE VHDDGRGIDP
     DVLRKKGIEK GLISADANLT RQDLFGLLFH PGFSTKEQVS EFSGRGVGMD VVKSNISALS
     GMIDMSSEVG KGTVMSLTLP ITLAIIKALV VRVKEKDYAI PLNSVLETLM LEPGMLQTIE
     GREVMELRQQ TLSLLRIDEL FKLDGQEKEG NRFVVVVGFA DKRLGIVVDE LRGQQDVVIK
     SLGKALDFVK GIAGAADLGN QKTILVLDVS GLIGEALQRE GGVGV
//
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