ID A0A0N1LF96_9SPHN Unreviewed; 777 AA.
AC A0A0N1LF96;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=IP68_10355 {ECO:0000313|EMBL:KPF75019.1};
OS Blastomonas sp. AAP25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Blastomonas.
OX NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF75019.1, ECO:0000313|Proteomes:UP000037930};
RN [1] {ECO:0000313|EMBL:KPF75019.1, ECO:0000313|Proteomes:UP000037930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP25 {ECO:0000313|EMBL:KPF75019.1,
RC ECO:0000313|Proteomes:UP000037930};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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 -!- 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:KPF75019.1}.
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DR EMBL; LJHP01000011; KPF75019.1; -; Genomic_DNA.
DR RefSeq; WP_054134908.1; NZ_LJHP01000011.1.
DR AlphaFoldDB; A0A0N1LF96; -.
DR PATRIC; fig|1523416.3.peg.436; -.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000037930; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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 InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037930};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..386
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 512..729
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 747..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 85537 MW; A6E6ACACEA435FF3 CRC64;
MLASSALPQP RKSRFARRFA VMMRKGSLFP VLEVGCVVLL ITMIGFSIWL VGSYQGRQAM
VPAPVTATLL VGNLVPAMAL LALIGRRVAI SRAGVSGEQG TGRLHVRFVA LFSLISSIPM
LLVVVITSLL FQYGVEFWFS DRARGMLENA NDLARGYYEE GRRDVSAETV AMASDLREYL
QQTRIDSPEF AEAYIFQVVG RKMNESAIVE IGDDGVIRTA AIVDPDNRTS SDRVTPDIVR
QLEAGETAVV SAEADRIEVV TPLDKKARVY LYVARASNQL ALSQWERAQT VLSDYKALFS
RSQNLQVQFN IALFVVSLLL VAVALWAALK FADRMVRPLT DMASAARDIS TGNFATRVDT
ANRTDEVGVL GRAFNRMASR LSEQTSALIR ANSQLDDRRA FTEAVLESVS AGVISVDPMG
MVRLMNSTAQ RLLLIDAEQC LGCTLSSIAP PFARLVGDGT EKAVIQYSRG TDLLTLAVRT
VREPYGLVIT FEDITQQLVD QRQAAWSDVA RRIAHEIKNP LTPIQLAAER LKRRYGKKVS
EDDPTFGQLT DTIVRQVGDL RNMVDEFSSF ARMPKPVFRE ENFFDLVRQA IFLQEVAHPA
IRFAAEGVHE GSDLHCDRRQ IGQAVTNILK NAVEAIEAKT QADEVYQGSV TATVSRQAQY
LVLTLDDNGI GLPADRDRIV EPYMTTREKG TGLGLAIVKK IVEEHFGDLA FESNDVGGTR
VIIRLDTDLL LASAGQDAAN AAPVIRHSSP DRASRIGATA DRRHNELSRT AQDEESN
//
