ID G8PTD2_PSEUV Unreviewed; 560 AA.
AC G8PTD2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=PSE_1153 {ECO:0000313|EMBL:AEV35665.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV35665.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV35665.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV35665.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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; CP003147; AEV35665.1; -; Genomic_DNA.
DR RefSeq; WP_014283959.1; NC_016642.1.
DR AlphaFoldDB; G8PTD2; -.
DR STRING; 911045.PSE_1153; -.
DR KEGG; psf:PSE_1153; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_5; -.
DR Proteomes; UP000005634; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR34220:SF10; SENSOR HISTIDINE KINASE BTSS; 1.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:AEV35665.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AEV35665.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..193
FT /note="Signal transduction histidine kinase 5TM receptor
FT LytS transmembrane region"
FT /evidence="ECO:0000259|Pfam:PF07694"
FT DOMAIN 366..444
FT /note="Signal transduction histidine kinase internal
FT region"
FT /evidence="ECO:0000259|Pfam:PF06580"
SQ SEQUENCE 560 AA; 61257 MW; 4D4F2B328A942E36 CRC64;
MALILHLLQQ MCVYLVIVYM VSKTPLFKIF TEDAPRLPHK ILIYLVFSGF CVIATTFGEQ
VDGAIANTRA MGAVLGGLLG GPVTGFLIGL TGGLHRYGFG GFTDLACAIS TTSEGLLAGM
TAFYLRTHNK RALLFRPMFV FGLTFVAEVV QMLIILIVAR PFDQALALVE QIAPPMLLVN
SLGAAFFMSI VRDQKTMFDK LSSAFSSQAL KIAERCVGVL AKGLNEVSGS KVAQIVKDET
NVGAVAITDR TKLLAFIGIG SDHHKPGTEI SSRLTLDAIE QNKVMYADGV EEPYGCSLSP
TCKLGSCLVI PLHSDTEVIG TIKLYEQKNK LFLNINRTLG EGIAKLLSNQ ILYGELEEKQ
SLLTRAELKL LQAQVNPHFL FNTLNTIAII TKRDAEKARE LLLQLSKFLR INLKRTSGLV
TLGEELDHVD AYLAIEKARF PDKLAVEVDV PTELLSLKIP AFTLQPLMEN AIKHGISQSV
EGGSVRISGA LVDGQVELQV EDDAGLYIPP KNREGLGVTL VDKRLKKQWG EKFGLHIEWE
EEAFTRVSIH LPAPVLEAAQ
//
