ID A0A1C5GTP9_9ACTN Unreviewed; 1222 AA.
AC A0A1C5GTP9;
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=GA0070613_0298 {ECO:0000313|EMBL:SCG36511.1};
OS Micromonospora inositola.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG36511.1, ECO:0000313|Proteomes:UP000198221};
RN [1] {ECO:0000313|EMBL:SCG36511.1, ECO:0000313|Proteomes:UP000198221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG36511.1,
RC ECO:0000313|Proteomes:UP000198221};
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; LT607754; SCG36511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5GTP9; -.
DR OrthoDB; 163538at2; -.
DR Proteomes; UP000198221; Chromosome i.
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 CDD; cd17574; REC_OmpR; 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; IPR035965; PAS-like_dom_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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SCG36511.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198221};
KW Transferase {ECO:0000313|EMBL:SCG36511.1}.
FT DOMAIN 357..573
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 627..742
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 887..1096
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 675
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1222 AA; 131313 MW; 62B5C32A17013B4A CRC64;
MSSAEGGEGG RRSSSGTGEA ELPPLLTAAF AAGGEMGERL RAFDWSTSPL GVPADWPAAL
RHAVSMMLSS RAQIVMFWDD EHRAFYNDAY RPTIGAKHPA VIGQPARVHW AETWAVLGPL
LDGVRRTGEP YRGENHPFVI DRHGFLEDVY FDVSYDPIRD ADGTVDGVFC FVNETTGRVL
GERRLRGLAE LGSQLADVRS TRELGQVAAR VLDGYRADVP FSLLWLYDAE GRPTLAGCSG
VDPGQVVGGP PEPPVAAADA PEKARPVPVG DLLGGLPPDA AEHALVLPIT ATNEPAGVLV
LGLARRLPLT DEYRDFTDLV AAQISRAVGN QRAYEQERAR AAELAALDRA KTNFFANVSH
EFRTPLTLVL GPLEDLLADP GLPAAYTERL TMMHRNALRL LKLVNTVLDF SRLESGRLAA
RYQPTDLADY TSRLASTFRS AIERAGLRLV VDCPPLPAPV HVDRDMWEKI VLNLVSNAVK
FTFDGEIRVR VRAVDGAARV EVIDTGVGIA PAELPHVFER FHRVPGVRSR THEGTGIGLA
LVRELVEMHG GTVEVRSRVD EGSSFTVTVP FGHGHLPADR VATLAPVPLT EPEQARRYVA
ETALWIDQVE PPAGLPEPAD APAGGGRILL ADDNADLREH VTRLLAHSYE VVAVPDGVEA
LRLAVDAPFD LVLTDVMMPR LDGFGLVTAL RANPLTRHVP IVLLSARAGS AEAVAGLSVG
ADDYLTKPFS SQELIARVRA NVELGQLRGQ IIRRLRALAD AAVAINNARS TADVVRVAAR
HALSLTEAAR VVVTATGARY EADGGGEAAA EPSAVLPLSG TTGEQLGELR VWRREHDRTE
EAALTQLARL VGVRLENAQL YEAEHRIATT LQHSLLPRTL PQLPGAVVAS RYLPGSADVE
VGGDWYDVIG AAGDELVLVI GDVVGKGVRA AAAMGQLRNA LRAYVLEGFD PGQALTRLNR
LVGSTEGGSF ATVVCLCFSP RTGRLRYASA GHPSPLLIRG DDVAFLHDRA LGPPIGAIPE
VAYPSVEGEL APGGRLLLYT DGLIEDRQLA IDAALDQLRL DAATRGEHVA DLVDAVVGRV
AGRPRHDDVA VLALEAAELN RFALRLPADP TRLSALRKRL EDFLIAHQVG EDDLFDLTVA
ISEAAANAIE HPVSPAEPVI WVEVMIEDRT VIATVRDSGL WRESAGSGFR GRGLALIKAL
GDLTLRRTAE GTEVTLRRQL RD
//
