ID G2FEJ2_9GAMM Unreviewed; 825 AA.
AC G2FEJ2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TevJSym_ai00410 {ECO:0000313|EMBL:EGW54761.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54761.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW54761.1, ECO:0000313|Proteomes:UP000005167}
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:EGW54761.1}.
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DR EMBL; AFZB01000009; EGW54761.1; -; Genomic_DNA.
DR RefSeq; WP_006474490.1; NZ_AFZB01000009.1.
DR AlphaFoldDB; G2FEJ2; -.
DR eggNOG; COG4252; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000005167; 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; cd00075; HATPase; 1.
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; IPR007890; CHASE2.
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; IPR017181; Sig_transdc_His_kin_CHASE2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PIRSF; PIRSF037347; STHK_CHASE2_PAS_prd; 2.
DR SMART; SM01080; CHASE2; 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 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:EGW54761.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Transferase {ECO:0000313|EMBL:EGW54761.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 529..583
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 658..809
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 803..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 90781 MW; 6D9E949333EE6D80 CRC64;
MSVANGTLRQ VKRLLLPLLL AGVMVLLAAS GWLWRLDNLL YDLQLGWRGS VAADDIMLVA
VDDQSLAEFG RWPWPRERHA QLIEILTRAG ARAIVMDLLF AEPDPANPQG DRRLIQAVAA
SGKVFMPVVV EELQLGGQLL ESLPLPQLTE VVAGLGHVHM ELDDDGIARG IYLQEGLGEA
FWPHLMLTVL QSLEPARFPP AEQSGPATMA AKRFSIVRQG HRLIPFAGPP GHFPRLSYAQ
VLRGAFHPDS LRDRIVLVGV TATGLGDVLP TPLSGRGQPM AGIEINANIL QSLRNGEAVK
PLARHWQLLL TGLLVALPLL LYSRLPPRLV PLLALGLILS LLLLSLMVLQ FGGIWFAPSA
ALLGLVLSYP LWSWRRLEQM VLHLDQELQR LSQGPQLLPA PNDLKDLQQG LESIAATLPL
QGWCVDDALG ARLAQAGRQP DPSDDLLQAG CWSRLGRSLW TLLPRGTQYW RLGLCWPPGE
LPRGRGQALL DDFVRQFSIP PAAASAKGSQ RLEQRIREVE AANQHLRQLR DFINTALGQM
DDGLLVLDSI GRVVLANPRA AFYLGLTHES ELHGQPALTF LKPLQIVGDL HWEPLLRELL
LRGDGCRFEA LRLPDTELFV QLRPLHPETA GMFGMIVTLS FIGTLKQSER ARARMVNFLS
HDIRSPLTSL LALTQSEQVL QAGSRELATQ VAPYARRALK LAEDFLQLAR AESVERSAFT
DTDFVSVAHN AVDEVYVQAQ ARNLCLQRQF EVEEVWLQAD AGLLERALIN LLSNAIKLAP
QDSQVEIMLR CDGDQLDCCV KDRGPGIPPG ASRGAVPAVQ ERPGP
//
