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Database: UniProt
Entry: A0A1H9W0L4_9ACTN
LinkDB: A0A1H9W0L4_9ACTN
Original site: A0A1H9W0L4_9ACTN 
ID   A0A1H9W0L4_9ACTN        Unreviewed;       551 AA.
AC   A0A1H9W0L4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04487983_103946 {ECO:0000313|EMBL:SES27344.1};
OS   Streptomyces sp. yr375.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761906 {ECO:0000313|EMBL:SES27344.1, ECO:0000313|Proteomes:UP000198568};
RN   [1] {ECO:0000313|EMBL:SES27344.1, ECO:0000313|Proteomes:UP000198568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR375 {ECO:0000313|EMBL:SES27344.1,
RC   ECO:0000313|Proteomes:UP000198568};
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; FOFF01000039; SES27344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9W0L4; -.
DR   STRING; 1761906.SAMN04487983_103946; -.
DR   Proteomes; UP000198568; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SES27344.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          310..519
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          146..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..230
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  58219 MW;  799109D63E0370C5 CRC64;
     MSGDGRPGRL KVYLGAAPGV GKTYRMLDEA RRRAARGADV VVGFAECHGR PRTEAMLDGL
     EVVPRARCVH RGGECEEMDL AAVLARRPQV AVVDEFAHRN VPGDGRNAMR RQDIEAETMS
     SLARSIVRGD ATIPALLERT RETFGMNSAE LVTEPPDAES LDPEPLDRSP LDAESSDAEP
     LAPSLLDAES SDAEPLASSP LDAEPPDPEP LDRPPLNAEP PAPEPPDAEP PDAEGVTAVT
     PVTAVTVVPA GPGAYLLLRG RSLSGSERRV LAAFAAHVGA AVERARLAEA VAEVEPVKAA
     DRMRTALLRA VGHDLRTPLA AGWAAVTSLR SRDVEFTPED RDELLATADE SMAKLSRLVE
     NLLDLSRLEA GVLPLNLRAT TLEEVLPTAL ADVPVAEARD VERIPAVLAD PPLLERVVAN
     LVGNAARHTP PGQQVLVTAS ALAGRVELRV VDRGPGLPAD GRERLFEPFQ RLGDTNNTTG
     LGLGLALARG LTEAMNGTLT PEDTPGGGLT MVVSLPCAQQ DEERRTDPDG RDAGRSEAGS
     PPFDEALATG L
//
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