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Database: UniProt
Entry: A0A1H1ZV69_9MICO
LinkDB: A0A1H1ZV69_9MICO
Original site: A0A1H1ZV69_9MICO 
ID   A0A1H1ZV69_9MICO        Unreviewed;       770 AA.
AC   A0A1H1ZV69;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04489721_3347 {ECO:0000313|EMBL:SDT37146.1};
OS   Agromyces flavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=589382 {ECO:0000313|EMBL:SDT37146.1, ECO:0000313|Proteomes:UP000199482};
RN   [1] {ECO:0000313|Proteomes:UP000199482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 202695 {ECO:0000313|Proteomes:UP000199482};
RA   Varghese N., Submissions S.;
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; LT629755; SDT37146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ZV69; -.
DR   STRING; 589382.SAMN04489721_3347; -.
DR   OrthoDB; 9757990at2; -.
DR   Proteomes; UP000199482; Chromosome i.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF13185; GAF_2; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          391..609
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          627..740
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          747..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         676
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   770 AA;  84349 MW;  C9701FE416B6D0B3 CRC64;
     MVGERDHPVD EERFRRLERD YNDATEQFVA MNEVLTALGR SSSDPDAVLD TVVESARRLC
     RCEAAQVYLI DGDQFVLSSS VGLSDEFVRY VDEHPFQRDR RTLIGRVTLD RKVQQIADVL
     SDPEYGRQDV QEIARYRTLV SAPMLLDDDV VGALSLWRSE VDPFDARAIA LLEAFAAQAA
     IVVRNAHLVR ELEQRSAELA RRVEQLEALS DVGAVVSSSL VLDEVLQNII MNAVRFSGCD
     GGSIMEYVEE ERCFSVRSAY ASSAELLRKL RGIRVELETT LVGRAALEGH PIAVADLDTV
     EHLDPHLKLL HDDGWRSVLA VPVLRGDRII GALVVRRKRP GAFSEETVEF LETFASQSAL
     AVWNAQLFRE LETKTAELQV VSQHKSEFLA SMSHELRTPL NAVIGFSEVL LERMFGELNE
     RQDEYLRDIL SSGRHLLQLL NDILDLSKVE AGRMELSTSR FSVRSVMEYG ISMVRERAGL
     HGIAVTLEVD PAVDGIESDE LRIKQVLVNL LSNAVKFTPD GGHVDVVARR DGDELAVTVT
     DDGPGIAPDD RERIFESFQQ GRRGPQREEG TGLGLTLCRR IVTLLGGRMW LESELGAGST
     FGFSVPMHRP APSSPVAQDG DGHHLPVIVV VDDDRASLDL MTAYLDGLGV RVVLGRDGNE
     GIELIRAHAP AAVILDIRLP GMDGWSVLTT LRDDEATRDI PVVIVSILDE RSRGLAHGAA
     DYLVKPVGRD DLVGALRRVG AVGASGTGVD ASTGPAADLP ASTPPGRGAS
//
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