ID I6EFZ5_SHIBO Unreviewed; 598 AA.
AC I6EFZ5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN Name=narX {ECO:0000313|EMBL:EIQ42937.1};
GN ORFNames=SB444474_1249 {ECO:0000313|EMBL:EIQ42937.1};
OS Shigella boydii 4444-74.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766140 {ECO:0000313|EMBL:EIQ42937.1, ECO:0000313|Proteomes:UP000004199};
RN [1] {ECO:0000313|EMBL:EIQ42937.1, ECO:0000313|Proteomes:UP000004199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4444-74 {ECO:0000313|EMBL:EIQ42937.1,
RC ECO:0000313|Proteomes:UP000004199};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (MAR-2012) 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 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:EIQ42937.1}.
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DR EMBL; AKNB01000202; EIQ42937.1; -; Genomic_DNA.
DR RefSeq; WP_000918033.1; NZ_AKNB01000202.1.
DR AlphaFoldDB; I6EFZ5; -.
DR PATRIC; fig|766140.3.peg.1391; -.
DR Proteomes; UP000004199; 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 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 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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..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"
SQ SEQUENCE 598 AA; 67098 MW; 6634D33B37E0D382 CRC64;
MLKRCLSPLT LVNQVALIVL LSTAIGLAGM AVSGWLVQGV QGSAHAINKA GSLRMQSYRL
LAAVPLSEKD KPLIKEMEQT AFSAELTRAA ERDEQLAQLQ GLQDYWRNEL IPALMRAQNR
ETVSADVSQF VAGLDQLVSG FDRTTEMRIE TVVLVHRVMA VFMALLLVFT IIWLRARLLQ
PWRQLLAMAS AVSHRDFTQR ANISGRNEMA MLGTALNNMS AELAESYAVL EQRVQEKTAG
LEHKNQILSF LWQANRRLHS RAPLCERLSP VLNGLQNLTL LRDIELRVYD TDDEENHQEF
TCQPDMTCDD KGCQLCPRGV LPVGDRGTTL KWRLADSHTQ YGILLATLPQ GRHLSHDQQQ
LVDTLVEQLT ATLALDRHQE RQQQLIVMEE RATIARELHD SIAQSLSCMK MQVSCLQMQG
DALPASSREL LSQIRNELNA SWAQLRELLT TFRLQLTEPG LRPALEASCE EYSAKFGFPV
KLDYQLPPRL VPSHQAIHLL QIAREALSNA LKHSQASEVV VTVAQNDNQV KLTVQDNGCG
VPENAIRSNH YGMIIMRDRA QSLRGDCRVR RRESGGTEVV VTFIPEKTFT DVQGDTHE
//
