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
//