ID A0A290QFQ8_9BACT Unreviewed; 1005 AA.
AC A0A290QFQ8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CMV30_04040 {ECO:0000313|EMBL:ATC63191.1};
OS Nibricoccus aquaticus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Nibricoccus.
OX NCBI_TaxID=2576891 {ECO:0000313|EMBL:ATC63191.1, ECO:0000313|Proteomes:UP000217265};
RN [1] {ECO:0000313|EMBL:ATC63191.1, ECO:0000313|Proteomes:UP000217265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-65 {ECO:0000313|EMBL:ATC63191.1,
RC ECO:0000313|Proteomes:UP000217265};
RA Choi A.;
RT "Complete genome sequence of Verrucomicrobial strain HZ-65, isolated from
RT freshwater.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP023344; ATC63191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290QFQ8; -.
DR KEGG; vbh:CMV30_04040; -.
DR OrthoDB; 184212at2; -.
DR Proteomes; UP000217265; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000217265};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 303..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..217
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 367..437
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 440..491
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 492..566
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 569..621
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 641..866
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 888..1004
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 343..377
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 475..502
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 939
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1005 AA; 111297 MW; 5F4842D43CCA7CE5 CRC64;
MLLTSLSRVL FRRRLSVVLL VAVGLAASYA LYLEARRNED LRVREDVKRR ADTRHILIRE
TMDGYVEGLH SLRNLTGALD LIDADKFQLI ARDTMERHPG FHALQWVPCP AAPDTSATAS
HSLTYLPVQF NQASPAAPSA TAAFSGYDYI TSPLARYFEN ARHTRRLVVT PVAELPALTG
EKSVLMIYPV FPGKNSASAT APCAGFVVGV FRVSTLFGES WKNFAGQIAD VMFLDATPGT
PASDRQMFYW AADNGPATTR ALTEAEFRAG SWYRELPLQL GGRVWLLLHR AKDGWFERQR
TNFPTIILVG GVLFTLVCAA YIRGAVRRAA LVEKEVHART AELRQTQALL EEDIQRREEA
ENLLRSSQQQ LHGLMENSPN AIFVKDPEGR YLSVNRRYAE LHARQREDFL GRSDFDVFPP
ETAARMRMSD ARVISTGQPV ELEDTFATAA GTHTSIVHKF PIIDEDGRVH GLCGIATEIS
ERKRAEAEIR ENRRQLESIL GQLPGMAFRM VQDGQLVPVY ISRGALGLTG HSARDFLEKV
VALHEIIHPE DRERARNAIA TAVKKRRSYE IEYRIVDRTG RIKWVLDRGQ GVYNEDGRLL
FIEGLAIDIT QRKDAESEKL IVERRLLEGQ KLESIGVLAG GIAHDFNNLL TGIIGNANLA
GLELPKTSPV HQNLKHIENA SLRAAELCQQ MLAYAGKGRF VIQRIELGPL VESTVPLLRA
SISKKATLKF QLQPDLPATM ADPTQMRQIV MNLVINASES LGEHDGVITL STSLVRPPAG
FFEGSVLTPP EPAADFLQLE VTDTGAGMTP DTVSKIFDPF FTTKFAGRGL GLAAVQGIIR
SHHGGLKVRS APGRGSTFTL FFPAASAVPI DPTPVRRATA TPWKQQGRAL IIDDEDHVLK
VTASLLQSCG MATELARDGY EGIDLFRAHP NDFDLVVLDM TMPRLSGEET LQLLREIKPD
VRVLFMSGYN RREVIASLGG TGELGFIQKP FTLDTLREQI QSMLS
//
