ID A0A1V4LVF9_9PSED Unreviewed; 497 AA.
AC A0A1V4LVF9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BZ163_05230 {ECO:0000313|EMBL:OPK11284.1};
OS Pseudomonas sp. VI4.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK11284.1, ECO:0000313|Proteomes:UP000189889};
RN [1] {ECO:0000313|EMBL:OPK11284.1, ECO:0000313|Proteomes:UP000189889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VI4.1 {ECO:0000313|EMBL:OPK11284.1,
RC ECO:0000313|Proteomes:UP000189889};
RA Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA Gawronski S., Vangronsveld J.;
RT "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT isolate from crude oil contaminated soil in Bobrka, Poland.";
RL Submitted (FEB-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:OPK11284.1}.
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DR EMBL; MULM01000102; OPK11284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4LVF9; -.
DR Proteomes; UP000189889; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
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 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OPK11284.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:OPK11284.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..484
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 55089 MW; DB85367AD3057BEA CRC64;
MQILEQHTTA ASQTPATERK GRRGPFNLLR WFSLGSFFII AAVALGLGSV STRFVVTESV
ERDSMLTAQF IQAMGEAEIR HAAISPNRTM GEMLDPRQDH GYPDVEPATR AAARIEFLDH
VEHLPDLLLA TVYALDRTVV WSTNPELIGV RIEGDEELDE SFTMKESVST SYHEIVEERP
EQRLLREPEY LFIENYIPMF NADKSQVIAM VEIYKEPVDL VARIQRGFKA IWLATVLGGA
AIYLALFWIV RRAAKLLESQ QKQLVSNETF VALGEMSSAV AHSLRNPLAN IRSSAELAQD
IASLGAQKNI GDIINQVDRM SRWVRELLMS LRPVNDDDET VDLVLAIDDT RGAFDALIKR
YGVEVRFTPQ GCPLVVSQKV LLTQILNSLF ANALEAMPKG GVLSIEIESP QPGRVCMTLS
DTGKGMNPQQ QQMVFKPFFT TKQGGLGVGL ALVKRIMERF DGSVELTSRE QEGTRVSLNF
IVATGGENGA QHTAGRG
//