ID C5T4I9_ACIDE Unreviewed; 653 AA.
AC C5T4I9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN ORFNames=AcdelDRAFT_1819 {ECO:0000313|EMBL:EER60595.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER60595.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER60595.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER60595.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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|PIRNR:PIRNR003167};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:EER60595.1}.
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DR EMBL; ACQT01000048; EER60595.1; -; Genomic_DNA.
DR AlphaFoldDB; C5T4I9; -.
DR PATRIC; fig|573060.9.peg.3304; -.
DR Proteomes; UP000003856; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR029095; NarX-like_N.
DR InterPro; IPR042295; NarX-like_N_sf.
DR InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF13675; PilJ; 1.
DR PIRSF; PIRSF003167; STHK_NarX/NarQ; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR003167};
KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR003167};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR003167};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003167};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR003167}.
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..248
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT COILED 240..267
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 653 AA; 71669 MW; A02920738E6459A1 CRC64;
MHVKSGFIAP SYTAPMRTKS PLTFKLLAMG GGFLLVALAS IGLTLWVAWK LEGGAAAVNE
AGRLRMNMLR MVLVQQTESP EEVQRHARQF DASLELLRTG DPSRPLFVPW GADTRERFEE
IRTTWGGLRK EWAVGLPPDR ARSLAQADSF VHKVDGFVEA IEIQIAGWTA VLHIFQLSMM
AVAIAAAITF MAVSYLLVLN PVSQLQQAQA RLRQGDLGVR LPVEADDEFG QLSAGFNLMA
HALQASHEEL EQKVREKTAN IAVQNQRLAA LYEVSALASS ATGLEALAQG FVKQIRRVAG
ADAAAVRWSD EANERYVLLA GDGMPVAMTE EEHCLHTGAC MCGQPQSQAR TRVIPIVPST
TLAFPHCRDA GFQTMVAIPV QMQQRLLGEI NLFFRSPTAH TDEVRDLLEA MTRHLASAME
GLRATALERE AAVAEERSLL ARELHDSIAQ SLAFLKIQTQ LLRDAVAKGD VVARDRSMGE
LDVGVRECYA DVRELLVHFR TRTSEEDIEA ALRATLSKFE HQTGIATTLT MAGHGLPLPP
DVQIQVLHMV QEALSNVRKH SGATRVELHV HRHPRWRFEV LDNGTGFRVD AVPPDSLHVG
LGIMRERAQR IGAVVQVESS PGEGARVCIE LPTMAALQAP RETPLPVLAE SEH
//
