ID F6IPP0_9SPHN Unreviewed; 723 AA.
AC F6IPP0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PP1Y_AT26089 {ECO:0000313|EMBL:CCA93392.1};
OS Novosphingobium sp. PP1Y.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA93392.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA93392.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(2011).
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}.
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DR EMBL; FR856862; CCA93392.1; -; Genomic_DNA.
DR AlphaFoldDB; F6IPP0; -.
DR KEGG; npp:PP1Y_AT26089; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_019564_1_0_5; -.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000009242; Chromosome.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR44936:SF9; SENSOR HISTIDINE KINASE GLNK; 1.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 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, ECO:0000313|EMBL:CCA93392.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..367
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 494..712
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 723 AA; 79881 MW; 36229A54B793595D CRC64;
MQVGARRANF FAMMEVLSVV AFLIMTATTW FALNNGADKG QLLPSNLTAS LLIGTLVPAM
AILVLLGRRM ALRRAAEHIG GTGRMHVRLV FIFSLISAVP TLLVVVFASW LFQSGVEFWF
SDSSRGLLEN ANKLARGYYE QTQRDVGYES VAMAEDARTM LSEYPIASPA FQAFYADQVY
RRNLSLSAII QVGPDGNQRT PIIVDPEGNS EDKRIGEDVL QRLEKGEPMV VTSNANKIVA
VVPIERDSGV YLYAARSNDL VSLSQGQHAE NIVQAYEVLS NRARVLQLRF NVALFVASLA
LVGLAVWFAL RFADRQVKPL YELVDAARSV GSGNFSLRIE GRTGADEIGL LNRAFNRMTA
QIEKQTQALL GVNRQLHERR VFIEAVLESV TSGIISLDEQ DRILLMNSMA LKLLTDRDKE
VPEGMALAEL APSLADLVEK GGAAGIVQYN RNGELLTLAV KTSRDATGHV ITFEDITRQL
LDQRTAAWSD VARRIAHEIK NPLTPIQLAT ERLSRRYRKQ IVDNPELFED LTRTIIRQVG
DLRKMVDEFS SFARLPKPVF RVEDPVALTR QALFLQEVAR PDIRFSFSSD PGIGTIDCDR
HQFGQAMTNV LKNAIEAIES KAKDAPEGWL GKVAVAVTAD EDHIVVRIAD NGIGLSQDRE
RIIEPYVTTR EKGTGLGLAI VNKIIEEHGG EMQFTPTEGG GTTVTMRFAT DPLAQSRKSE
AAE
//