ID A0A0M2LWE8_9SPHN Unreviewed; 453 AA.
AC A0A0M2LWE8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=XM50_06090 {ECO:0000313|EMBL:KKI20233.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI20233.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI20233.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI20233.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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};
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:KKI20233.1}.
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DR EMBL; LAZX01000085; KKI20233.1; -; Genomic_DNA.
DR RefSeq; WP_046408229.1; NZ_LAZX01000085.1.
DR AlphaFoldDB; A0A0M2LWE8; -.
DR STRING; 1642949.XM50_06090; -.
DR PATRIC; fig|1642949.3.peg.3288; -.
DR OrthoDB; 9815202at2; -.
DR Proteomes; UP000033997; 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; cd00082; HisKA; 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; PTHR45436:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..226
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 234..449
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 453 AA; 48417 MW; 6A28044211D97784 CRC64;
MPDRAHTVRQ ITLFFTAGFA LVTLLLGAGA YLLGEDVVHE QLDAQIIAET RALRAVAEEG
DLAALMEALR RRDDRGVNSF GYLLTAPDGQ RLGGELVTEA LGEGWHDIRF RDPDGEGHPA
RSLVTRLPGG LQLTVAMESD LPVQLRNRLL FLFALGLVLL VAIAIVGSAL FGRTIIGRLN
TINRIASAVS RGQLDARIPV SQQNDEFDQL AATLNDMLDR NAAHIVNLRR VSSDVAHELR
TPIMRLRLRM EQSLADAGEG TPEAAAIERS IADIDSILSL FAALLRIAEV EAGGLRAYFR
PVALTATVEA LAESYALAAE DGRRALVTRL EPGITVNGDR DLLAQIVVNL LENALRYTPP
GTRITLSLTS GKDSAHPTAE LTIADDGPGI AEADRARALQ PFERMASGGS GHGLGLSLVA
AIVASHGGTI ELADNAPGLS VRIILPRMQK AAH
//