ID A0A0G1CV47_9BACT Unreviewed; 460 AA.
AC A0A0G1CV47;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UV19_C0009G0009 {ECO:0000313|EMBL:KKS53493.1};
OS Parcubacteria group bacterium GW2011_GWA2_42_28.
OC Bacteria.
OX NCBI_TaxID=1618822 {ECO:0000313|EMBL:KKS53493.1, ECO:0000313|Proteomes:UP000034375};
RN [1] {ECO:0000313|EMBL:KKS53493.1, ECO:0000313|Proteomes:UP000034375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKS53493.1}.
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DR EMBL; LCDN01000009; KKS53493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1CV47; -.
DR Proteomes; UP000034375; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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 PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKS53493.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..224
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 239..457
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 460 AA; 52346 MW; 1280BC8A3EB51537 CRC64;
MGILCSAFAI FLALLGMMYY YLQIEKDDIL RQNNLLAQVM THEIESGYIK GIWPYKTLKM
VSDEEEVVFL WIAQPDGKVF WTDDPGIMGK IVQDPFLGIT EMQSRDSLYD GQRIKLIAHP
LKIELSEKPW TLFLGVSFKQ LAKAQMEIMA FSVIFFAIAI SFSAFISLYL SGSFTRPLRK
LMVGVEAIGQ GDLDYHIDVN TKDEISDLAA AFNQTAKKLK ETRERDKQIS QMKSDFISLA
AHQLRTPLSM IKWGLSLIRE NVLNEEEKST VYQKVDASNE RMISLVNDLL NVTRIEEGKF
DYKFSAGQLT ETLQMAVDEL RNEADRRKVK LIFNIPSCQL PKIQIDKDKM RIALTNIIEN
AIKYSLPGGQ VEISLICHKS DILITIRDQG VGIPKAEEKR VFEKFFRGSN AVRLETEGSG
LGLFMAKNII EHHGGQISFK SKQNQSTTFF IILSLERQVK
//
