ID G2DEN3_9GAMM Unreviewed; 850 AA.
AC G2DEN3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Rifp1Sym_cd00080 {ECO:0000313|EMBL:EGV50915.1};
OS endosymbiont of Riftia pachyptila (vent Ph05).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV50915.1, ECO:0000313|Proteomes:UP000004491};
RN [1] {ECO:0000313|EMBL:EGV50915.1, ECO:0000313|Proteomes:UP000004491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(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 -!- 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:EGV50915.1}.
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DR EMBL; AFOC01000057; EGV50915.1; -; Genomic_DNA.
DR AlphaFoldDB; G2DEN3; -.
DR Proteomes; UP000004491; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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 Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGV50915.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EGV50915.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 375..446
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 627..843
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 850 AA; 95403 MW; 3E404EAAEF333EC9 CRC64;
MPDRTPRWYR PWIERVPLPW MSVLVGLLCG LIVWLVLDPL QSRALGEIFQ KELQQQLEQR
ARDSRHRFQQ YLGQWRLTAT GLAQNWRLVE YVKSPAWAQE REKPKTYLNR LPAWMAPAPV
SLGAVTPSQI VLLDQDLEPR EIFHRQDLPF PLERAASRYP GGDGALLTTL WKAPFLLVWA
GVAQPVESKA AILMLIIPLD TIFLLDSQQA VADDETVVAL LEGDQQRILA SSDQTKVTAN
MLLEQLRSRY LITSQSITDF ADWDQNVQFS TFVSRKRVEA TAERILSTER RERFLGALAF
VGVFSLLFFL VSMRLHRLLN RIASFGRRAL GINQPVSEKG NQLLLLEAWI PDFFALVSEA
VEQARLRHEL QIRESEALKS ALLDSSLDSI VTVDCSGMVV ETNGTAERTF GYTREQMLGE
SLGVKLFHPD DRQQFGKLLQ RYNQSAELVA ASAPLQLRAF DAQGDEMPVE TVVMPILLEH
TTLFTVYIRD ISARRRAERE IESLATFASD NPSPVLRVNR RGVITYANAA SAPLLAYWSL
EPQQTLPLYW RNLVLETLEE GGVREIELSG DEQIFSLLLA PFSEQEYVHI YGRDITQVRN
AEQQSRQHQS ELVHVCRVST MGEMATGLAH ELNQPLAAIV NFASGCVRRL QAGIGGEAEL
VDAMAQITVQ AERAGEIIKR LRSLVGKNAS EHTLVNLNDL VIEVASFIEY DAAKKGVDVR
LALEQGGLPV RVDLVQIEQV LLNLMRNAMD AMQQTEADQR ILVLSTSRLN VREVAVMISD
TGPGIPPEVM EKLFDPFFST KQSGMGMGLA ISYRIIEDHN GSIRVTSEKG KGTLFSVQLP
SNPDLKLPGL
//
