ID A5W5Q7_PSEP1 Unreviewed; 795 AA.
AC A5W5Q7;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Pput_3341 {ECO:0000313|EMBL:ABQ79467.1};
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:ABQ79467.1};
RN [1] {ECO:0000313|EMBL:ABQ79467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ABQ79467.1};
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};
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DR EMBL; CP000712; ABQ79467.1; -; Genomic_DNA.
DR AlphaFoldDB; A5W5Q7; -.
DR KEGG; ppf:Pput_3341; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_6; -.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABQ79467.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ABQ79467.1}.
FT DOMAIN 7..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 434..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 682..791
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 562..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..151
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 398..428
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 730
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 795 AA; 88448 MW; D1751613AE808D63 CRC64;
MQQTPLKILM VEDSSMDAEL TLMRLERSGL HVQSQLVFDH AGVEHALRQA RYDLILCDCV
LPGSSGTEVL AIAQRLAPDI PFIFLSGIYG EEHAVEMIRL GATDYVLKKN LPLLPKAVRR
ALSEVQERQR RRRAEEALAD VEARARIAID AAGMGTWDLR PQEGLLLWDD RCKTLFGVPT
STEMSLEVFY AGIYPDDLPL VREAVEHAMR PESGGHYRVE FRIAQPNGLE PRWLLSSGQS
QFVDDQCVRF SGVLQDIHTQ RQATQALRQL NEMLGERVER RTRERDRAWE LSQDLLAVLN
KDLTPVALNP AWEASLGFSR ERLSQSSLLH LLPEHDQEQL LTELAALSHG RTSARFVGRI
LHAGGQQRWL SWVVVPEDTL LYVVARDITS EREAALGLAD ANARLREQIN ERERIEAALQ
QMQRLEAVGQ LTAGVAHDFN NLLTVILTGA SFLERDLAKA DLDKARTRLT HIREAGERGA
KLTSQLLAFS RRQRLEPVPL NLNRTLAGLE ELLRRTLGGN VSVRLDLDLA LWQALTDPTQ
TEMIILNLAI NARDAMPDGG QLTLTTRNTH IDQRPQRPED PDPGEYVMLS IRDTGCGMSE
DVLAKVFEPF FTTKDIGKGS GLGLAQVFGF AKQSGGGVRI DTILGRGTEV AVYLPAVKEE
MVNEPVAAVL SQSISESGHN RTVLLVDDDH LVRDMLGDVL RQYGYQVRQA HSGEQALALL
DDDIDLLLTD FAMPEFNGAQ LALAARERYP RVPVVFLTGY AELQGLELPG SLVIQKPVQA
DELARALNEM LGISG
//
