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Database: UniProt
Entry: A0A1H2CMH1_9ACTN
LinkDB: A0A1H2CMH1_9ACTN
Original site: A0A1H2CMH1_9ACTN 
ID   A0A1H2CMH1_9ACTN        Unreviewed;       559 AA.
AC   A0A1H2CMH1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04489716_6233 {ECO:0000313|EMBL:SDT71710.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT71710.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT71710.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT71710.1,
RC   ECO:0000313|Proteomes:UP000198688};
RA   de Groot N.N.;
RL   Submitted (OCT-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; LT629758; SDT71710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2CMH1; -.
DR   STRING; 113562.SAMN04489716_6233; -.
DR   Proteomes; UP000198688; Chromosome i.
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; IPR007891; CHASE3.
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; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF05227; CHASE3; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDT71710.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..267
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          303..517
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          524..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          255..300
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        524..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  60649 MW;  758008D3E945B098 CRC64;
     MRISVRHWTL RVRIFALCAA TGIILGGLGV VAALTAAANN RQIDNVLDRA SPMRAAGETL
     STALVNQETG VRGYAITGQD RTLEPYLRGL AAETDQVARI QRLLGPEDDE IRAALDTVVA
     RAATWRANVA EPLLETVRTE GTQAAQQRVE ASDTRDFDAL RGAVSVMQDR ISVLRASSAQ
     AARDSSQTMV AIEVAAAVII LITGVLLLIL LDRLVSRPIL HLAGQVRQVA AGDYTRHIDS
     TVYGSPDLIG LADDVDQMRQ QIASELSEVS DARQQVEWIN QQLRTQAEEL TRSNRDLEQF
     AYVASHDLQE PLRKVASFCQ LLQRRYAGQM DERADQYIGF AVDGAQRMQR LINDLLAFSR
     IGRLTTGFTD IDLNELLSDV KSQLSGRAGG EDAEISWTGL PTVEGEEPLL STLFVNLIGN
     SLKFHRPDVP SQIRISAELD GSEWRINVRD NGIGIEAEFA DKVFVIFQRL HARDAYDGTG
     IGLAIVKKIV EYHGGRIWLD VDVAEGASIW FTLPVVPGLS PVLPASSASS TSPASSASSA
     DSLPAGSDSS SGEEEKVGM
//
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