ID A0A0G3CTF1_9GAMM Unreviewed; 582 AA.
AC A0A0G3CTF1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, 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=QQ39_16490 {ECO:0000313|EMBL:AKJ43970.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ43970.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ43970.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ43970.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(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};
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DR EMBL; CP010423; AKJ43970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3CTF1; -.
DR STRING; 82985.QQ39_16490; -.
DR KEGG; pfq:QQ39_16490; -.
DR PATRIC; fig|82985.3.peg.3420; -.
DR Proteomes; UP000068021; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AKJ43970.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000068021};
KW Transferase {ECO:0000313|EMBL:AKJ43970.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 308..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 366..579
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 582 AA; 64873 MW; 01F9FC78C2A2D812 CRC64;
MVMFCCSALA QVPTTTEVET INVGVLATRG DRAAIERWQP LMDWLTARIP NAHFQLHPYT
LEQMAAVVKS QDIDFIITNP GQSVQLGRQY PLSWLATLRS RYQEGTSQAI GSAFVVRSDS
PYQHLSDMKG KSVAAVSKIA FGGYLTLKRE MQQAGHDPER FFSTIDFTGF PLDAIIYKLR
DGDVEGAVLP ICQLEDMVRE GLIAGKNYRV LDNQVPDGFP CQASTRLYPN WSFAKTGKTS
EALAKQISRA LLALPEDHPA AIAADSLGWT TPISQLTVDK LYQDLDIHPL QNPWWKEALV
WLKANQQWGW LLIILIVVLN GYHFLLEYRF NKNQKRLLRV QNELNEKIAM LEHAQRVAIV
GELGASIAHE ISQPLAAIQN YSQGGLIRVN KGKPVTELQP VLEHIQHQVM RASDIVQRLR
GLINKRASEK KWSDVADIID DTLLLLRYEL EKSAISVTVS HEGEGRPVWI DPVGFQQLIL
NIIKNAIDAC NQACSPSATI AIELVFTPQQ LVVRVTDSGE GFAVEPALLQ SAFYSTKAEG
LGLGLAICRD VVKSHHGHME MCNVAPHGCR VEVTFPFIDN EQ
//