ID G2FAW2_9GAMM Unreviewed; 1079 AA.
AC G2FAW2;
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=TevJSym_aa00430 {ECO:0000313|EMBL:EGW55900.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55900.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW55900.1, 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:EGW55900.1}.
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DR EMBL; AFZB01000001; EGW55900.1; -; Genomic_DNA.
DR AlphaFoldDB; G2FAW2; -.
DR PATRIC; fig|1049564.3.peg.41; -.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5001; Bacteria.
DR Proteomes; UP000005167; 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; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
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 Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGW55900.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EGW55900.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1079
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003428712"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..257
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 279..330
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 452..506
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 526..577
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 578..651
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 650..702
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 715..938
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 960..1076
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1010
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1079 AA; 121197 MW; 309BBCAED58303BB CRC64;
MIVTLIVVAA MAILAASSAV ALRIANKSAP LIDASMEVKY ELSLFHLWFE ELVQQDPTVD
KEQVWQHLNQ ARWYANTMLQ GGESSHVKFQ ALDDPALRSM IRNTLDQIDR LEAVGLARLK
RAQSSLAGSN QDQLFDKVFA EVLKIADDVE TAVYRNMATQ IRQFERLVYI LGAVVMLVGL
AGGILFFLIE RRRRSDYTLL QESETRFRRL FENTAAISVQ GYDRNRRVIY WNPASEALYG
FTADEAIGQQ LEDLIIPGEM REGMIAAIDA WIDDGTEIPS SEITLRRADG SPIQVFSNHV
MLRTHNNEPE MYCIDIDLTE RKRAEAQARQ HELVLNSVFQ ALPDLFFLMD QDGTIRDYRA
PQAADLYVPP ETFLGKRMQD VLPPTLAAQF NENRAVVSER GGLTTYEYTL ELPHGLRLFE
ARLSQLPDSP QLIAVIRDIT ERRRAEEALA KSAQEWTHAM DFFEDAIYLI DLDDKLVRAN
QAFYKLTGLT PELAIGMEIT SIIHPQKEAE PCPVCAARIA RSDKYITMEA NHPHNPTGRP
IEVMVRTIRD DTGSPLGVLM GMHDLTRARQ AQQALRESEE RYRTIFEGAP EGVWLIGPDH
RTLEVNQRLC EMLGYRADEM IGRTPLDFAD EENQKIFRGQ AAKIETTDRR NYEVELRHRD
GHNIPAHFNA ITLHTDKGGV LASVAFVTDL TEQKITEQAL RRAQKMDAIG QLTGGIAHDF
NNLLGIIIGN LDFLKRLLPE DDKSLKRVES ASKAALRAAD LTRQLLGFSR KQAQEARPTN
INQVIRDMDS LIARSVTPEV EVELQLADHP WLTRIDPGDL EDALLNLILN ARDAMPQGGK
LTIETANKRL DKTYAGLNPA ITPGDYLQLA VSDTGSGIPK EILEQIFEPF FTTKPSDKGT
GLGLSMVYGF ARRSNGYVKA YSEPGIGTTI RIYLPRSIEK SEMIPQTSIS ETRLTPGHGT
ILVVDDEDNL LDLARDYLEE TGYKVHTATR ATEALALLES EDDINLLFSD VVMPGGMNGY
ELAEQAYKLY PNLKILLTSG FTKKVAARHS QAHFAANLLS KPYSRDDLIK RIQDVLDGE
//
