ID A5W970_PSEP1 Unreviewed; 991 AA.
AC A5W970;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Pput_4560 {ECO:0000313|EMBL:ABQ80680.1};
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ80680.1};
RN [1] {ECO:0000313|EMBL:ABQ80680.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ABQ80680.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000256|ARBA:ARBA00006434}.
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DR EMBL; CP000712; ABQ80680.1; -; Genomic_DNA.
DR AlphaFoldDB; A5W970; -.
DR KEGG; ppf:Pput_4560; -.
DR eggNOG; COG0591; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_22_1_6; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd10322; SLC5sbd; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:ABQ80680.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ABQ80680.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 630..678
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 763..978
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 991 AA; 109259 MW; 230EBCD04BE45647 CRC64;
MPMSFSLTQM ILISAGYLMV LFGVAWISER GLIPRSIIRH PLTYTLSLGV YASAWAFYGS
VGLAYQYGYG FLACYLGVSG AFLLAPVLLY PILKITRTYQ LSSLADLLAF RFRSTWAGAL
TTIIMLIGVL PLLALQIQAV ADSISILTGE PVKARVAFAF CTLIILFTIF FGSRHIATRE
KHEGLVFAIA FESVIKLLAL GGIGLYALYG VFGGPHELEV WLLQNQTALA ALHTPLQEGP
WRTLLLVFFA SAIVMPHMYH MAFTENLNPR SLVSASWGLP LFLLLMSLAV PLVLWAGLRL
GASTNPEYFT LGLGIAANNQ ALALLAYIGG LSAASGLIIV TTLALSGMAL NHLVLPLYQP
PAEGNIYRWL KWTRRALIVA IITAGFMFYL SQNYHQSLAN LGIVAFVATL QFLPGVLSVL
YWPTANRRGF IAGLLAGTLV WMVTMLLPLL GNLQGFYIPL LDMIYVLDDT SWHMAAIASL
AANVLLFTLI SLFTNASTEE VSAAEACAVD NVRRPQRREL HAASPQEFAT QLAKPLGAKA
AQKEVEQALR DLYLPFDERR PYALRRLRDR IEANLSGLMG PSVAQDMVET FLPYKSGNEN
YVTEDIHFIE SRLEDYHSRL TGLAAELDAL RRYHRQTLQE LPMGVCSLAK DQEILMWNKA
MEELTGIAAK HVVGSRLVTI DEPWRGLLQG FINVPDEHLH KQRLALDGQP RWLNLHKAAI
DEPLAPGNSG LVLLVEDLTE TQALEDKLVH SERLASIGRL AAGVAHEIGN PITGIACLAQ
NLREEREGDG EIIELSSQIL DQTKRVSRIV QSLMSFAHAG GSHQNSEEPV CLAEVAQDAI
GLLALNRRNF EVQFFNLCDP DHWAEGDPQR LAQVLINLLS NARDASPPGS AVRVRSEVNE
HTVDLIVEDE GSGIPKNIMD RLFEPFFTTK DPGEGTGLGL ALVYSIVEEH YGQITIDSPA
DIERQRGTRI RVTLPRHVVA TSPEIRDRRE N
//
