ID A0A1J1LE83_9CYAN Unreviewed; 1100 AA.
AC A0A1J1LE83;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PL9214290343 {ECO:0000313|EMBL:CUR30752.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR30752.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CZDF01000132; CUR30752.1; -; Genomic_DNA.
DR RefSeq; WP_072717731.1; NZ_LN889782.1.
DR AlphaFoldDB; A0A1J1LE83; -.
DR STRING; 671072.PL9214290343; -.
DR OrthoDB; 337251at2; -.
DR Proteomes; UP000184315; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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 Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00331; PP2C_SIG; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CUR30752.1};
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:UP000184315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUR30752.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 380..432
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 454..676
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 719..836
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 424..454
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 769
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1100 AA; 123400 MW; F73EF4DDCACA8942 CRC64;
MSIRLPQVQL IWFKIVRKSR HPIPIRTVLI VPFLLQIFGA VGVVGWLSFQ AGQKSVHEVV
SQLQNEISAR VEQNLEAYLT VPEKINQTNL NLIRSGTLTL KNLNSWEKYL WGQVQIFPEI
NFIKVTNAAG QERTGEQLGD GSLRINVVDT FTNFDFYSYQ TNNKGDRTKV ATIVKDFDTR
KGVWYQDAVK AGGTTWSSVY LSLLEPTLLM SALLPVYNPQ TQQIQGVLNT ALRLDGIGDF
LNRLKVGKSG QTFLIDSKGT LLATSTLEKP FQEINNERQL FPAINSKNLL TQATAKYLSQ
TQGNLNNIKQ GKDLEFTWNR ERYFVKVLPF QKGKTVNWLI LVVVPESDFM EQINTNTRTT
IILCSLALLG ATVIGLLTAQ WIVKPILQLN IAAKQIAQGN WEQTVNLKRK DELGQLGRSF
NRMAKQLKES FTILEAKNKE LQDLDQLKDE FLANTSHELR TPLNGIIGIA ESLIEGVTGD
LPSETNSNLA MIVASGRRLS SLVGDILDFS KLRHKNIELQ LRPVDVYSIV NAVSILSQPL
ITQKDLHIIN RIPAEFPLAE ADENRLQQIL YNLIGNAIKF TSEGIVEISA RILSETEKPQ
MAITISDTGI GIAADKLERI FESFEQAEGS TAREYGGTGL GLTITKQLVE LHGGKITVQS
ELGIGSQFTF TLPIAENTIK NPSENRVKNL SKPLQINPLI AINPNFSKPF MDYSPETIKI
LIVDDEVVNR QVLFNNLSLN NYAVFQATNG EEALELIEHG LKPNMILLDV MMPKITGYEV
TQKLRERFNA TELPIILLTA KTQVQDIVTG LNMGANDYMM KPFAKDELLA RIRTHINISR
LHAENLRLAT ELEVTRRLQQ MILPKPEELA TIHELEILGF MEPAEEVGGD YYDVLETDGV
VTLGIGDVTG HGLESGILML MTQTGIRTLK EVRETDPIQF LSILNRTLYK NVERMNVDRN
LTLVLLNYYQ GLLTVSGQHE EILIVRSNGT IERIDTMDLG IPIALDEEIT EFIDSTTVEL
KAGDGVVLYT DGITETFNLS KEQYGLNRLC NVISKNWHNP IEDIKQAVIN DVVMFRGEQK
QFDDITLLIL KQKAHVKDSA
//
