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Database: UniProt
Entry: A0A2K8SPM3_9NOSO
LinkDB: A0A2K8SPM3_9NOSO
Original site: A0A2K8SPM3_9NOSO 
ID   A0A2K8SPM3_9NOSO        Unreviewed;      1093 AA.
AC   A0A2K8SPM3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=COO91_03326 {ECO:0000313|EMBL:AUB37381.1};
OS   Nostoc flagelliforme CCNUN1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB37381.1, ECO:0000313|Proteomes:UP000232003};
RN   [1] {ECO:0000313|EMBL:AUB37381.1, ECO:0000313|Proteomes:UP000232003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB37381.1,
RC   ECO:0000313|Proteomes:UP000232003};
RA   Shang J.;
RT   "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT   its photosynthetic adaptation to extreme terrestrial habitat.";
RL   Submitted (NOV-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; CP024785; AUB37381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8SPM3; -.
DR   KEGG; nfl:COO91_03326; -.
DR   Proteomes; UP000232003; Chromosome.
DR   GO; GO:0016020; C:membrane; 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; 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; 4.
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; 2.
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; 4.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000232003};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          170..226
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          395..446
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          447..517
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          519..571
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          572..631
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          647..698
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          723..941
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          972..1090
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1021
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1093 AA;  122025 MW;  9A6CB8897AA6865C CRC64;
     MVTELAVPLG GSKLRAASRR EVRATPTHCL ADFGNNPLAS CIQGEATLKG TRSLLAPYAV
     TLLAVGSALL LTLLLQPLLK PPIFLLFFPA VAVSTWYGGM KAGLLATALS TLAVSFFFLE
     PVFSLVVDNL DSIVRLGLFM LVTTLISLLT SELGTAKQDL QMSLQKLQMS EAKFRRLVES
     NIIGVIVANM DGAIAEANDV FLTMVGYSRE DLLAGRVRWR DMIPPEYIEA NNSAMPTAGY
     AYAELKTKGV CQPFENEYIR EDDSRVPILL GCALLENNPE HVICFVLDLS ERKQVELALS
     KSEERYRAFL EQSSEGIWCM ELEVPISPDC PEDEQIQHFY QYGYLAECNN VMAQMYGFSR
     AEEIISTRLG DFLVPSDPDN IAYLCNFIRS NYRLIDAESH EIDKQGNSKY FLNNLVGIVE
     NGLLVRAWGT QRDITERKQV EAALRQQEDQ LRLITNAVPV QISYVDGEQR YRFNNKGYED
     WFGIPTSEIY GKHIREIVGE SVYESILPYI ETVLSGQQVT YETQVPDKDG TNHYVNVTYV
     PQFSQQGKVE GFVALITDIT LHKLAEAAVK QSEKRLKTLT EKVRVIPWEV NVTTGNFTYV
     GPQTVDILGY QLSDWYTDDF WAKHMHPEDQ EWAIQYCQES SLSLNNYEFE YRMLAADGRV
     VWLFDIVNVV RDENGPQLLH GFMIDITDRK QAEQEREQLL ERERTARADA EAANRMKDEF
     LATLSHELRT PLNAILGWTQ LLRNRKFDET TTSRALETIE RNTRSLAQLI EDVLDVSRII
     RGTLHLNIHR VKLVPLVEAA IDTVYPAAQA KEISINCKFD PEIGVVAGDA NRLQQVVWNL
     LSNAVKFTPK GGRVDVQLER IESYVQIRVS DTGVGIAAEF LSHVFERFRQ EDSSITRSHG
     GLGLGLAIVR HLVELHGGTV SAESPGIGQG ATFIVNLPMK AVYVEANTAE QLSSVADTQD
     VNNYLPNLDG LRVLIVDDEA DARHLLTMIL GQYGAQVMAA PSASDALLAL QEFRPHILVS
     DIGMPQEDGY TLIRQVRALP TDQGGRIPAV ALTAYARAED RTQALLAGFQ LHVPKPVNPA
     ELAAVVANLT GRT
//
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