ID A0A1Z4JN67_LEPBY Unreviewed; 1132 AA.
AC A0A1Z4JN67;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES2135_50230 {ECO:0000313|EMBL:BAY58150.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY58150.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY58150.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY58150.1,
RC ECO:0000313|Proteomes:UP000217895};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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; AP018203; BAY58150.1; -; Genomic_DNA.
DR RefSeq; WP_017289769.1; NZ_AP018203.1.
DR AlphaFoldDB; A0A1Z4JN67; -.
DR Proteomes; UP000217895; Chromosome.
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; -; 2.
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; 3.
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; 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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13188; PAS_8; 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; 2.
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; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAY58150.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000217895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 566..618
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 619..675
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 765..983
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1007..1125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1056
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1132 AA; 126199 MW; 4629AF993603D4A4 CRC64;
MNQQTDPYHD HSSPEQAQLM LIEQNRLLKL VASGQPLETC LTEVCHSIAQ LNPGTHACFL
IADAQRVSFL QVIAPNLPAA FRQRLEGALI NEFCIGSFGD AMYRGQPVSC PEIANDDRWS
SEWRSLCVAH NILACHSEPL IGLNHLPFGL LMLCFEQARI RTDWEFQLAQ FSTQIASIVF
ERDRTDLVCQ DREKQYRTLF ESIDEGFCIC ELLLNQNGEP QDYRLLEVNS AFEKLTGLEQ
ATGKTARELV PNLEDFWLET YAQVVQTGKS IRFEQESIAL GHWFDVNAFR IGEPQRHQFA
LLFTNVTERK QAEKLSRQAT EIETFRVSLV DALRPLAHPV EVQATASRML GEYLNVTRVV
YFEVQGADYV VERDYVNGAD ALAGRYAIES FGEKVLKAYR AGQTTSASDV TADPNLSPEQ
HSAYAAIQIK AHIGIPLIKN GEFVAGLAVH NATPRVWLPQ EIALAEEVAE RTWAAVERAS
AEAALRNAHK QLESALAAGA VYTWRWNIPA YRVIIDAKFA RLLDIDAAVA TTEGLPIETF
INWMHPDDRV LGFAALQQAI TTGEAYTSEY RVQLATGEKR WFTARGQVEY DATGNPIALL
GALADMTVAK RLEESRRRAE EDRDRFFQLS QDMLAIVHMD GYFLQTNPAW ETTLGYTLPE
LTAQPYIEFV HPDDRAATVA AADLIAQGIP LHEFENRYRA RNGSYRWISW SVAPFIEQKL
MYCVARDMTD RKSAEVEREQ LLQQTQVAKE AAETANRIKD EFLAVLSHEL RSPLNPILGW
TRMLQTGRLN APQTQQALAT IERNATLQAQ LIEDLLDISR ILRGKLVLNV VSVDLASIIR
AALETIRLAA EAKNIQIQTM FEGTRWRVSG DVARLQQVVW NLLSNAVKFT PEQGRVEIRL
SEVGHHAQIE VSDTGKGISA EFLPYVFERF RQEDGSTTRQ FGGLGLGLAI VQQIVELHGG
TVNVSSPGEH QGATFTVTLP LEQIESPSLP NSSELFAIAH ASLVGIHVLI VDDEPDARDF
QAFVLEQRGA IVTVVDSAIA ALQQLNQVMP DVLLSDIGMP NMDGYTLMQL IRSRPPEQGG
MIPAIALTAY VGELNQRKAI EAGFQKHFAK PVAPDLLIQA IADLVNISNS SA
//
