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Database: UniProt
Entry: A0A1C6SLR1_9ACTN
LinkDB: A0A1C6SLR1_9ACTN
Original site: A0A1C6SLR1_9ACTN 
ID   A0A1C6SLR1_9ACTN        Unreviewed;      1216 AA.
AC   A0A1C6SLR1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=GA0070616_4079 {ECO:0000313|EMBL:SCL30461.1};
OS   Micromonospora nigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL30461.1, ECO:0000313|Proteomes:UP000199699};
RN   [1] {ECO:0000313|EMBL:SCL30461.1, ECO:0000313|Proteomes:UP000199699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL30461.1,
RC   ECO:0000313|Proteomes:UP000199699};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; FMHT01000003; SCL30461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6SLR1; -.
DR   STRING; 145857.GA0070616_4079; -.
DR   OrthoDB; 163538at2; -.
DR   Proteomes; UP000199699; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SCL30461.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199699};
KW   Transferase {ECO:0000313|EMBL:SCL30461.1}.
FT   DOMAIN          352..568
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          619..734
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         667
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1216 AA;  130359 MW;  DBBA4FA178A13E81 CRC64;
     MSSAQGGVDG GSPSGTVDAI PPLLVAAFAG GGEMGALIRD HDWAVSPLGT PDRWPAALVS
     AVGMMLASKS QIAMFWGEDL RAFYNDAYRP TIGDKHPHVL GQPAREHWAE TWEILGPVLA
     GVFRTGESYQ GRDHHFLLDR HGFVEDVYFD VSYDPIREAD GSINGVLCIC SETTGRVLGE
     RRLRTLAELG SKLADLDSGA ELGRAAATVL DRHRADVPFG LLYLRDHDGH LRLAGRSGPA
     PGVAEPTRAL VEAAATGVAG TISVADLLGH VPPDAADEAV VLPISATNER AGVLVLGVAR
     RLPLGDEYRD FLELVAAQIS RAVGQQRAYE QERARAAELA ALDLAKTNFF ANVSHEFRTP
     LTLVLGPLED MLADPELPEA YPQQLTMMHR NALRLLKLVN TVLDFSRLES GRLAAHYVPT
     DLSNYTARLA STFRSATERA GLRLVVDCPP LPTPVYVDRD MWEKVVLNLV SNAVKFTFDG
     SIRVSVRAVD GAARLEVADT GVGILPEEMP HVFERFHRVP GVRARTHEGT GIGLALVREL
     VEMHGGRVEV RSRVDEGSTF TVTVPFGSAH LPAERLGDGS PAEDELHQAR LFVAETALWS
     AGADAPQPAA RPAAGARGRI LVVDDNGDLR DHVTRLLAPS WEVVTAGDGL EGLRLATHDP
     FDLVLTDVMM PRLDGFGLVT ALRADPRTRY VPIVLLSARA GSAEAVAGLA VGADDYLTKP
     FSGEELVARV RANVELGQLR GQIIRRLRAL ADAAVAVNTA RSTADVLQVA ARHALSLAEA
     DRVVVSATGA RCEADAGDAS SVEPSFVLPL TATAGEQLGE LRVWRPVTDE VGTDEAALAQ
     LARLVGVRLE NAQLYEAEHH IATTLQHSLL PRTLPQLPGA VVASRYLPGS ADVEVGGDWY
     DVVAVGEDEL VLVIGDVVGK GVRAAAAMGQ LRNGLRAYVL EGFDPGESLT RLNRLVGSTE
     VRSFATVFCL WYSPRTGRLR YASAGHPSPL AIRGGDVAFL HDRALGPPVG ALPDTVYPTV
     SGELAVGDRL LLYTDGLIED RHLGIDAALA QLRVDATRPG EHVADLIDAV VERVAGQPRR
     DDVAVLAMEA AELNRFALCL PAEPTRLSVL RKRLEDFLLA HGVGETDLFD LTVAVSEAAA
     NAIEHPVDPA EPTIDVDVRI EDRTVIATVH DSGRWRESTG AGFRGRGLSL IRALGELTVS
     RTAEGTDVTL RRRLRD
//
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