ID A0A2I0CMF7_9PSED Unreviewed; 910 AA.
AC A0A2I0CMF7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CW360_13610 {ECO:0000313|EMBL:PKF70334.1};
OS Pseudomonas pharmacofabricae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1905276 {ECO:0000313|EMBL:PKF70334.1, ECO:0000313|Proteomes:UP000242861};
RN [1] {ECO:0000313|Proteomes:UP000242861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZYSR67-Z {ECO:0000313|Proteomes:UP000242861};
RA Yu X.-Y.;
RL Submitted (DEC-2017) 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 -!- 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:PKF70334.1}.
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DR EMBL; PIYS01000027; PKF70334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0CMF7; -.
DR Proteomes; UP000242861; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PKF70334.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000242861};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PKF70334.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..910
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014184841"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..622
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 639..761
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 783..902
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 693
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 832
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 910 AA; 100304 MW; F9686C6FCDBDB08B CRC64;
MHWPSTALRL LACLLLCLSS SLPAVADALH WRSLVDEHNT LQLKDIRSSR YQVQFSDTPL
QQLAMPGRDK SLWLQVSLPA SEQTRLLRLF APQLQQLDLY LVQDDQALLQ LSTGERPRQP
VNAQPGPDYL FNLPPLQAPA ELYLRLAANH SLRPTLQLTE ASQLVDSQPQ PLLLGMLLGA
CVMLILYNLV RYAYARTRCG LWLGAAQGGL LLSCASLFGL LPAPHPDWAW LHASLSELLV
LVTLGCSLMF TRSFFHQVCA EQYGQRWLAA AGIIVALAML IQAGDLLAEQ WLFLLVLLGT
LCMLSIAASH WRHGYRPARL FTLAQLLFCS SLLIASPAFL GYWPVSSATL LGGLLASAIA
SHFLLSLALS ERQRRILHSD FSHSRARTAN RAELRAKAEF LAHISHEIRT PMNGVLGMTE
LLLDTALSAK QRDYVQTIHS AGNELLGLLN EILDFSRLES GQIELDEVQF DLNALFEDCL
DVFRSKAELQ QVELISFMQP QVPQVIKGDP ARLRQALLSL LEHAFRHTQG GEVLLLATLD
EQTPPCLRIT VQDSGQALSN EERQALLGDT PHSKDLLSHP QLSSRLGLVI ARQLLRLMGG
DFGIQPGSGR GNTLWLSLPL RHPASQPASL LSGPLQGAQL LVVDDNDTCR KVLQQQCSGW
GMQVSCASSG TEALAMMRKR AQLNQYFDLV LIDQEMPGMS GLQLATRIKE DSYLSRDSLL
IMLTGVSQAP SKVNARNAGI RRVLAKPVAG YTLRATLADE LSQRPAASEQ PAPTALEIPS
DFRVLVAEDN SISTKVIRGM LAKLNLQPDT ASNGEEALQA MQRQHYDLVL MDCEMPVLDG
FTATERLRAW EAQTGAPRTP IIAVTAHVLS EHKEHAQAVG MDGHMAKPVE LLQLRELLAH
WIAQKHPPQA
//
