ID A0A2R5FLB4_NOSCO Unreviewed; 1240 AA.
AC A0A2R5FLB4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, 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=NIES4072_32380 {ECO:0000313|EMBL:GBG19570.1};
OS Nostoc commune NIES-4072.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2005467 {ECO:0000313|EMBL:GBG19570.1, ECO:0000313|Proteomes:UP000245124};
RN [1] {ECO:0000313|EMBL:GBG19570.1, ECO:0000313|Proteomes:UP000245124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4072 {ECO:0000313|EMBL:GBG19570.1,
RC ECO:0000313|Proteomes:UP000245124};
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 -!- 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:GBG19570.1}.
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DR EMBL; BDUD01000001; GBG19570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5FLB4; -.
DR Proteomes; UP000245124; Unassembled WGS sequence.
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; 4.
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; 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; 4.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
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; 4.
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; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
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; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 4.
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:GBG19570.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000245124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 257..303
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 377..433
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 502..572
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 821..1075
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1097..1215
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1146
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1240 AA; 138740 MW; C06D19ACCAEE9176 CRC64;
MMVKVLEKIL MMRSWLLTYS VMILAVIAAL LLTRLLLPVF DPSVFTLFYA AVAISAWYGG
MRLGVLAIAL SVTTAFYFLI EPVYSFDFLS PNVLVRLTSF SLVSFLITAL SSELRTARRK
AETSLKLLQN SEMRFSRLAE SNIIGVIVTD MNNGSIIEAN GAFLKMVGYT REDFAANKMN
WRDITPHEYL ILSERSVEEL RKTGVCKPFE KEYICKNGDR IPVLLGSVVL GDTQETVIGF
VVDLSEGKQA QAALQQANER NTRTLENMSD AFITLDRDWR IIYQNAEAER INGKSRTEVI
GKSYWEEWPL SVDTNVELQY RRAIAEQIPV HFEHHYYLPS KCDLWLEIHA YPCEDGLDIF
FRDISQRKQV EKAAQASEER LKSFFQANIV GILFADVNGR ITEANDEFLR IVGYTQADIQ
SGRLRWTDIT PPEYQYLDEL AIAEATAKGT CTPYEKECIR KDGSSVPVVV GYSLLGESQQ
NSVAFILDIS DLQQVKKALS QSQEQFQAFM DNIPAAAWIT NADGRVLYLS PTYLSTFDIA
TNKAINKNIF DLYPAQIAQP FLDNIRMVSQ TNQVFEAIES APRTDGTLGE FLVYKFPIAN
ASGQRLVGGV AVDITERERI LRERQLAEQA LQDRSERLKL LSETTSDLLS TERPLDLMNS
LFSKLSAQMD LHFYFHYLIE THENNQKLRL VGWNGITDEV FQAIQYLEFN QGICGQVAQE
RHQIVLNDVP HSTYPNADIL KALGITAYAG QPLIAQGKLL GVLSFASRTR TRFTSGEIAL
LQATSDQVAV AMERAQLMDS LQQQKEQLVQ ANRIKDEFLA VLSHELRTPL NPILGWSKLL
QTKKYDQATT TRALETIERN AKLQTQLIED LLDVSRILQG KLSLNIAPVN LETAIASAIE
TVRLAAQAKS INLRFTILDF GLQNPHRNLD INFNNQTDNL KSQIQVALPT SDRYDPKFLV
TGDSGRLQQV IWNLLSNAIK FTPQGGQVEI SLQSVGSQAE LRVSDTGKGI SPDFLPFVFD
YFRQADGATT RKFGGLGLGL AIVRHIVELH GGTVKAESLG EEQGATFTVM LPLMKTHFNS
HQIDRQLDDS PDLNGVKVLL VDDERDTREL IAFILEQSGA VVTQAASAME ALRIIPEFQP
NLLLSDIGMP EVDGYMLIRR IRAMLPEQGG TIPAIALTAY AAEADSQQAI AAGFGQHITK
PVEPAKLVRA IANLICSCSN LKTNLQSLEA RKRHNSLTNE
//
