ID A0A0C1NGC7_9CYAN Unreviewed; 1320 AA.
AC A0A0C1NGC7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DA73_0209570 {ECO:0000313|EMBL:KIE11896.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11896.1};
RN [1] {ECO:0000313|EMBL:KIE11896.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE11896.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
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:KIE11896.1}.
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DR EMBL; JHEG02000037; KIE11896.1; -; Genomic_DNA.
DR STRING; 1479485.DA73_0209570; -.
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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..386
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 439..509
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 512..564
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 882..1161
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1192..1317
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 855..882
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1241
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1320 AA; 147520 MW; 3A806E86F8A1F12E CRC64;
MLRVSRLHQQ SSHQLSSHSV VARAASAIAA SFGLLVFIGW WLNQKWLTSF LSFGTGSMEV
DTAVCFFLSG ISLWLSLKEE RDKKETIALT VISKVCAIVV LTIGLLRVSH YVFHWDLRVD
ALLHSDFLNG LGVIHWEGMG INTALNFIVL GRALELVNQP KTRRNYWYAQ VFSLIAALIS
LQVIIGYAYG VSILYSFPSQ DEGMALNTAL IVTVLCVGIL AVHPNEGLMR LITSDTYSGV
LARRLLLAAI AVPLVLGWIA LQGLRARWYE PELAVSLLVV VLIVSFCVLI WESAAALEKL
GKQRDRVQQA LKVNEEKLSS FVDSNVIGIL FGDIHGRVRN ANDEFLRMIG YTREDLQADK
IKWTDITPPE YLPLDAERIS EAISKGACTP YEKEYIRTDG SRIPVLVGYT LVGENREESV
AFILDLSVRK QVEQALRQSE ERFRLALDNI PDVFAIYNGK RQLEFVNAAA LQRIKKPKEE
IIGRTDEELF PPDVTKPYLS TLIQAQETKT LQKIEVVMNL PDYGEFTTEI KYLPLLDKKG
NIEQILAFTN DITERKQVEE TLRNQQKWLE DLLNLMPMPM LLIEPGTAKV TFANVAADKV
AGGKFPKAES QEDYKTYYYA TDAAGNPIPL EEAPGVRVAR GERIEGFELD WHTPVGIRSL
LIFADTLPAM HGYPATCVLV FQEITNLKQV EKALSLGYKR LQLLFGTASD LLSSQQPVAL
IDSLFKKLAQ QIRLDTYFNY LVYEDKQILQ LASYTGVSEE QVKEIEWLEF GQGVSGTVSQ
QRQPIALENV QQLTDTKTEF LRSIGITAYY SYPLIAQGQL LGTLAFGSLT RVKFTQNEMG
MMQAVCDQIA IAMERAKLIA SLQQQTEQLK EANRMKDEFL AILSHELRSP LNAILGWTQL
LRSRRQLDET KVSKALETIE RNAKAQTQLI EDLLDISRMI RGKLRLNVRP CNLVSIIETA
LETVRLAAET KEIDLKFYVL GETGQETGDR EENTQKFRNQ ASCLNMKGAS YNDIRNPSLT
SLSPALSSQF TVIGDSERLQ QIIWNLLSNA IKFTSQGGHV EVRLSVVKHK ESLRDLNSQF
PLSYVQIQVS DTGIGICPDF LPYVFDRFRQ ADSSTTRSFG GLGLGLAIVS HLVELHGGIV
SVESPGKGQG TTFTVKLPLL GKKDEEDREI RGQADRETRG TFTATPSLLG IRVLVVDDET
DTRDFLSIVL QQCQAEVKAV GCVREALEVI AQWRPDVLVS DIGMPNEDGY TLIREVRSLE
RTGKIPLSEQ GAKIPAAALT AYARTEDRLR ALQEGFQIHL PKPVEPAELV TVVASLAGRT
//
