ID Q4FU45_PSYA2 Unreviewed; 707 AA.
AC Q4FU45;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 136.
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:AAZ18463.1};
GN OrderedLocusNames=Psyc_0603 {ECO:0000313|EMBL:AAZ18463.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ18463.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ18463.1, ECO:0000313|Proteomes:UP000000546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC {ECO:0000313|Proteomes:UP000000546};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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}.
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DR EMBL; CP000082; AAZ18463.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4FU45; -.
DR STRING; 259536.Psyc_0603; -.
DR KEGG; par:Psyc_0603; -.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_000445_20_10_6; -.
DR Proteomes; UP000000546; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd16917; HATPase_UhpB-NarQ-NarX-like; 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:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 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; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000000546};
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 33..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..296
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 495..696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 707 AA; 80260 MW; 5CB54ADEB8F5F127 CRC64;
MLPNHYSPSC FLIGKSLLIM NSRLLRHSLP LHAWGAIFTI SILCFISTLG GGMLAWVSET
DAQAINTAGS IRMATYRISF QLATNFSENN PFDLNIGLKK NDLEGKKEGT ENVKGENRIG
EQDKLSPIRK EKTEEISTLI EDMESRLAEL HDYQLANAND NEGINNQLKQ IESQWFRELK
PALLSQDAQK FYIVSFKYIE DVDSFVNELQ YRNEQRQTWQ QILQIVSLVL TVIIMLVGMQ
RLRQNVLIPV QQLIKANYKF KQGKRNTKVS ISGYTEFNAL GDSFNDMAST IETHQRSLES
EVQIKTQHLV KANQVLSLFY DFSKSLTTSQ VSLYRLDTLI TDFGKILPHL EFTLCIQNKF
INNKNAIILH GEKMKELCKK LNCDNCLTKE GVYTKSYPIA HQKVEFGELK VRPKSVLLIN
STLFPNNNDG NTPSSQRIQI AKEGRTFFES EIGSELDLEN NELIVALTNL ISTALSLRKQ
RQQEHQLILF EERSTIAREL HDSLAQSLSY LKIQISVLER HLKNGSDEQN EASVRQHIDQ
IKAGLSSAYQ QLRDLLITFR LTIDNDNFDE ALHEAANEFA LKGKFEITVS NRVMTLNLSA
TEQIDLIQIA REALSNISRH AQAENVEIDL GYDDEDKYIV MTIVDNGVGI SGTVDQTQHH
GLMIMKERAH NLGGELIVSN NESQGTTITA KFAPNFFDEN ISKEAYL
//
