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Database: UniProt
Entry: J7QNN4_METSZ
LinkDB: J7QNN4_METSZ
Original site: J7QNN4_METSZ 
ID   J7QNN4_METSZ            Unreviewed;       625 AA.
AC   J7QNN4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=BN69_1547 {ECO:0000313|EMBL:CCJ06998.1};
OS   Methylocystis sp. (strain SC2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ06998.1, ECO:0000313|Proteomes:UP000005263};
RN   [1] {ECO:0000313|EMBL:CCJ06998.1, ECO:0000313|Proteomes:UP000005263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:CCJ06998.1,
RC   ECO:0000313|Proteomes:UP000005263};
RX   PubMed=23045511; DOI=10.1128/JB.01446-12;
RA   Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT   "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT   Methanotroph with High-Affinity Methane Oxidation Potential.";
RL   J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ06998.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7QNN4; -.
DR   STRING; 187303.BN69_1547; -.
DR   KEGG; msc:BN69_1547; -.
DR   PATRIC; fig|187303.17.peg.1684; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   eggNOG; COG5278; Bacteria.
DR   HOGENOM; CLU_000445_114_51_5; -.
DR   Proteomes; UP000005263; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16919; HATPase_CckA-like; 1.
DR   CDD; cd19410; HK9-like_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; 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   Kinase {ECO:0000313|EMBL:CCJ06998.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:CCJ06998.1}.
FT   DOMAIN          254..478
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          504..619
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         554
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   625 AA;  68406 MW;  1271FFFDCB8DC264 CRC64;
     MKMTVTVTLP KKAVSWAIFG FLVAAIGGAA ISLQKQVAAQ TWVEHTLYVR TALLQTLSTV
     QDAETSQRGF LLTGDDTFLE PFRNADRTIG ERLHALERAI SDNEEQMQRL KRLRSVVADR
     LAALQKHIQE RGASPDATFA DRLKNGKRLM DQARSIIAEM LGEEDRLLTT RNAEMRWTLT
     LTQMGVAGAL LSAALLGWAT LKDRQRQVVE LQTANAALRI ALKQAADESE RRERVEGQLR
     QSQKMQAVGQ LTGGLAHDFN NMLAVIVGCL NLLKRTMARG EVDKDGLIDK AMECVDRAAA
     LTHRLLAFSR QQPLAPQTVD ANKLVGGMAE MIRRTLGEAV NVETVLASGV WRIHVDPNQL
     ESALLNLAVN ARDAMNDEGK VTIETSNAYI DDHYAREHAE VKEGQYVLVA VSDTGAGMPP
     EVIAKAFEPF FTTKGPGKGT GLGLSQVFGF VKQSGGHIKI YSELGQGTTV KIYLPRFVGE
     GEVAAPIHQA NQLQRAMRGS PEMLILVVED EDRMRSVAVA MFKDLGYSVL AAGNAAEALA
     LINANPHIDL LFTDIVMPDM NGRALAEEAL RRRPDLKVVF TTGFSRNAVI HNGVLDRGVN
     FLPKPFSIEQ LAQKMSAVLG VMETT
//
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