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Database: UniProt
Entry: D7DZB7_NOSA0
LinkDB: D7DZB7_NOSA0
Original site: D7DZB7_NOSA0 
ID   D7DZB7_NOSA0            Unreviewed;       537 AA.
AC   D7DZB7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Aazo_5029 {ECO:0000313|EMBL:ADI66138.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI66138.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI66138.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI66138.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI66138.1; -; Genomic_DNA.
DR   RefSeq; WP_013193147.1; NC_014248.1.
DR   AlphaFoldDB; D7DZB7; -.
DR   STRING; 551115.Aazo_5029; -.
DR   KEGG; naz:Aazo_5029; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_39_3; -.
DR   OrthoDB; 5401154at2; -.
DR   Proteomes; UP000001511; Chromosome.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADI66138.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW   Transferase {ECO:0000313|EMBL:ADI66138.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        181..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          274..531
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          202..265
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   537 AA;  61635 MW;  894D8CE5B9980068 CRC64;
     MHLFYKLKFT PSQLVSLTVL LTLLLFIPQV WLNWQAYYNF NNIAKQEFHL QKLSNEITYL
     DEVLTMSARM NAATGNILWE KRYRQFEPKL DLAIKEAIKV GPETYKDQNP QKIDIANQQL
     IAMEYKSFDL VNKNQKQAAQ KILSSRKYET QKHIYTDGIA KRNKNISLAL EQKVAEYRQG
     MIWAILGSIL SLTILIPIWI LVLRLLQEYL KAKKNAQAAL EETNYMLEMQ VATRTASLNQ
     KNLQLQKTLQ ELQQTQVQLI QTEKMSSLGQ LVAGVAHEIN NPVNFIYGNL IHVREYTQNL
     LTLINRYRQE NSNYNPEINI LIEEIELDFL IDDLPKILSS MAVGAERIRE IVLSLRNFSR
     LDEAEMKPVN IHEGLDSTLL ILQDIIKGQE EQQEILIIKD YGNLPLVECY AGGLNQVFMN
     IIVNAIDALR QQEIDSSKDI NKHFSSIIIH TQVRNDEKVI INIQDNGIGI GETVKNKLFE
     PFFTTKPVGK GTGLGLSISY QIIVDKHKGK IECISEPEKG TEFVIEIPIR QIKPANT
//
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