ID A0A0L0GQ17_9ENTR Unreviewed; 598 AA.
AC A0A0L0GQ17;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN ORFNames=GM31_03225 {ECO:0000313|EMBL:KNC91057.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC91057.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC91057.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC91057.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(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 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:KNC91057.1}.
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DR EMBL; JNGI01000134; KNC91057.1; -; Genomic_DNA.
DR RefSeq; WP_049857702.1; NZ_JNGI01000134.1.
DR AlphaFoldDB; A0A0L0GQ17; -.
DR STRING; 379893.GCA_001297775_01416; -.
DR PATRIC; fig|379893.4.peg.665; -.
DR OrthoDB; 9811306at2; -.
DR Proteomes; UP000037393; 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 CDD; cd22900; NarX_sensor; 1.
DR Gene3D; 1.20.5.1930; -; 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; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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:SF51; NITRATE_NITRITE SENSOR PROTEIN NARX; 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; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 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:UP000037393};
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 155..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..228
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 393..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 220..247
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 598 AA; 67715 MW; DB34E94E5DED1BE7 CRC64;
MLKRRFTPLT LVNQLVLIVL LSTLIGVTGM TISARLVHGV QGSAHAINKA GSLRMQSYRL
LASIPLTAED QILLDNMEAT VFSPELEQAA IRDGQVEQLS ALQKYWQGEL APGMKKAHSQ
ATVAGDVASF VNRIDQLVYA FDHTTEERIT SVVSAMRWMV LVMALLLIFT IVWLRARLMH
PWQQLLRMAR AVSQRDFTQR ARISGRNEMA TLGMALNNMS EELAESYAVL EQRVQEKTAR
LEQKNEILAF LWQANRRLHS SIPICERISP VLNDLQGLTL LRDIEVRVYD TEDEENHQEF
TCHSESSCDE KGCFLCPREL PSPPGGGSTL KWRLTDAHNQ YGILLATLPE GCHMSHDQQQ
LVDTLVEQLT STLALDWHQE RQQQMIVMEE RATIARELHD SIAQSLSCMK MQVSCLQMRG
EALPMESRDL LAQIRNELNT SWAQLRELLT TFRLQLTEPG LRPALEASCI EYSAHFGFNV
QLDYQLPPRY VPSHQAIHVL QIVREALSNA LKHAQATVVK VTVYQQEHQV KLIVEDNGCG
VPDHAERSNH YGLIIMRDRA QSLRGDCQVR RRDNGGTEVV VTFIPEKSLS IQQGDTYE
//
