ID A0A1Z4JSL3_LEPBY Unreviewed; 955 AA.
AC A0A1Z4JSL3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES2135_65530 {ECO:0000313|EMBL:BAY59676.1};
OS Leptolyngbya boryana NIES-2135.
OG Plasmid plasmid2 {ECO:0000313|EMBL:BAY59676.1}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY59676.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY59676.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY59676.1,
RC ECO:0000313|Proteomes:UP000217895};
RC PLASMID=Plasmid Plasmid2 dna {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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP018205; BAY59676.1; -; Genomic_DNA.
DR RefSeq; WP_017291670.1; NZ_AP018205.1.
DR AlphaFoldDB; A0A1Z4JSL3; -.
DR Proteomes; UP000217895; Plasmid Plasmid2 dna.
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; 3.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 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; 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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
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; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 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; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; 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; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAY59676.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:BAY59676.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217895};
KW Transferase {ECO:0000313|EMBL:BAY59676.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 279..353
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 356..409
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 417..464
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 498..551
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 576..794
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 816..951
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 262..289
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 865
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 955 AA; 106291 MW; A483B4446C547CA7 CRC64;
MVTRTITAKL QRFFPAQFDL EIQASVWRYS IALLAVAAAL SITLLLDPLL RGTPAALFFV
AVMISSWLGG FGAGLFATLL STVALNYFFL EPLYSLDLAN LRAVFQLSVF AIAAILISSL
NEAQRSAKKR ADANLKAWRD SEAQFAHLSE ANIIGIFQAD RNGSITEAND TFLQMLGYTR
EDLLSGRIRW NEIVPPEYQE ATQRSEWNQC SHAQQERCTT DVCTPFETEY IRKDGARVPM
LLGSVTRDEQ TVIGFVLDRG EFKRNEAERQ QAEAALRERE QRLDLATSAA NLGVFEWNIQ
TDYAVWENAR MYEIFGRTLA EGTLNKVEFI NNVIHPEDRE AFELKLAESM MQNSSFQGVC
RIRRHDKGQW CWAEFSGQFD LAPDGTPLRL IGVIGDISDR KQAEAEREQL LHRLETSLGQ
LEAVINHMAE GLVVADPQGN ILTFNPAALA IHGYDSLEQV QRHLHKFPET IEVHDLQGSF
VPMEQWPIAR ALQGETFSNC EIQAHRRDIG RTFIGNYGGT PVRDKQGQVI LAIVTLRDVT
QQRHAQAELA RSLVAEQTAR EEAERANRIK DEFLAVLSHE LRSPLNPILG WTKLMQSQKF
SPERAAQALA TIERNAKLQA QLIEDLLDVS RILQGKMVLN ISSVNLATTI EAAIETVHLA
AEAKNIEIHT ALNDNESVVS GDAARLQQIV WNLLTNAVKF TPQGGRVEVR LDHCDRFAQI
QVQDTGKGIS PDFLPYVFDY FRQEDGATTR KFGGLGLGLA LVQHLTEQHG GTVRAESAGE
GQGATFTVRL PLQSFPSATD LERFPTTSTA DLHNVNILVV DDEADTRDLM LTILEAQGAQ
VKVVASATEA LTILAQWQPD VLISDIGMPE IDGYMLMRQV RLFEASQREL PSAQPGGRIP
AISAKRNCVA IALTAYAGEL DQQQALSAGF QQHLAKPIEP DKLIEAIVNL LDRLR
//
