ID A0A433SBK7_9BURK Unreviewed; 630 AA.
AC A0A433SBK7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RUS66115.1};
GN ORFNames=CUZ56_02193 {ECO:0000313|EMBL:RUS66115.1};
OS Saezia sanguinis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Saezia.
OX NCBI_TaxID=1965230 {ECO:0000313|EMBL:RUS66115.1, ECO:0000313|Proteomes:UP000286947};
RN [1] {ECO:0000313|EMBL:RUS66115.1, ECO:0000313|Proteomes:UP000286947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNM695-12 {ECO:0000313|EMBL:RUS66115.1,
RC ECO:0000313|Proteomes:UP000286947};
RA Medina-Pascual M.J., Valdezate S., Monzon S., Cuesta I., Carrasco G.,
RA Villalon P., Saez-Nieto J.A.;
RT "Saezia sanguinis gen. nov., sp. nov., in the order Burkholderiales
RT isolated from human blood.";
RL Submitted (JAN-2018) 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:RUS66115.1}.
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DR EMBL; PQSP01000006; RUS66115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433SBK7; -.
DR OrthoDB; 9792869at2; -.
DR Proteomes; UP000286947; 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; 1.10.8.500; HAMP domain in histidine kinase; 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; 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:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR Pfam; PF13185; GAF_2; 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.
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:UP000286947};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..236
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 430..624
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 228..255
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 630 AA; 71460 MW; 754B7126EBBA1A0D CRC64;
MKKPLYSLST KLLVSIIIWL IGAVSFTGLT LNLSWELENG GVAINDAGSL RKRMYHMAAL
ASQVGQQQDI FREQTDFETV VDRLERINTQ SWLNPENGEI HQRLQDIRLT SRQIIEQFLK
AANTGDLSLA LLHRTQDFIT QIDALVKAIE IQNTKNIRLL RLFQFILIGM VIFSAFVAIF
FLGRLVIRPL DILKTGIQKI SHGDLAARVI PISHDEFGEV SDGFNQMAAN LSDLYDNLEL
KVKEKTLALE EKNHELQLLY EITAFLHESQ TQENMAKGFL KYIMDICQAK AGSIRILEKG
KKQLDYISSI GLPESLVNSE TAAPSEKILG GISAHQSNII IQHIDPNDPQ FRDAGLLPFD
HSVIFYIRHN LKDIGILTLY FEHDHHLTEQ DIRLIETLTN QLGVSIENQR WALLEKQLGI
VEERNLMAQG LHDSIAQSLS FLNMQVQMLE NALREHNREQ ALENLKFIQE GVQESYDDVR
ELLLNFRTRI NQEDFPQAVQ SVINRFQKQV NIPVDLHISD SESQLNIEQQ LQAVFILQEA
LSNVRKHAQA RHVRVDICNN DDFVMTIDDD GVGFDAQTLL SKKDRHVGMG IMHERAARAN
GNVSISSPHA RKGTRVMLTI PISGAKRSTP
//
