ID K9ZET4_ANACC Unreviewed; 1042 AA.
AC K9ZET4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Anacy_1620 {ECO:0000313|EMBL:AFZ57122.1};
OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ57122.1, ECO:0000313|Proteomes:UP000010474};
RN [1] {ECO:0000313|Proteomes:UP000010474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP003659; AFZ57122.1; -; Genomic_DNA.
DR RefSeq; WP_015213771.1; NZ_AP018166.1.
DR AlphaFoldDB; K9ZET4; -.
DR STRING; 272123.Anacy_1620; -.
DR KEGG; acy:Anacy_1620; -.
DR PATRIC; fig|272123.3.peg.1770; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR OrthoDB; 569347at2; -.
DR Proteomes; UP000010474; Chromosome.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ57122.1};
KW Membrane {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:UP000010474};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ57122.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 371..535
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 576..801
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 826..949
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 539..576
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 875
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1042 AA; 117582 MW; BD4E06369ACF3F5A CRC64;
MQTILWELFP RFLVDNSYMP HGHCYLWQTP LVGLHLVSDA LIAIAYFSIP VMLIYFVRKR
SDIPFSKVFI LFGAFIVLCG IGHLLDIWTL WHPDYWISGI ERAMTALVSC YTALQLIELL
PQFLALRTPE HLESINKELE KQIAERQRTE ETLEMIVAGT ASVTGNDFFP ALVQNLATAL
NVSYALVSKT VNNSTPSLRT LALWAVSNLA ENIEYELTDT PCQKVVENRV LCSYPSQLQE
LFPHPPLLKN MDAQSYVGLP LLDINQNVIG NLCIIDVKPF IVDERTTTLL NVFAARAAAE
LQRQWAEEEK DHAYEELEFR VEERTAALVK ANNALESEIS ERIAAEVAMR AMAEREQAIN
RVILRMRQTL NLESIFNITT TELRQTIECD RVLIYRFQPD WSGELVSESV NQKWNILLPG
RAKDPKLTQT AVDQPNCVTT KLSTTDVLSH DTYLQDNKGG MLRQKNTYCC VNDIYTAGFD
SCYLNLLEEL QARAYIITPI FCGKKLWGLL AVYQNSNSRN WQQAEIGIVT QIGNQLGVAV
QQAELLAQTQ QQAEELKRAK EAADAANRAK SEFLANMSHE LRTPLNAILG FTQLMQQDKS
LTIDYQRYIE IINQSGEHLL ALINDVLEMS KIEAGRISLY KTEFDLHKLL YSLEAMFLMK
SQSKGIQLRF NCDISVPQHI KTDENKLRQV LINLLGNAIK FTEKGSVSLR VSSQESFTGD
AGRENILLFA IEDTGPGIAV EELSDLFQAF QQTQAGQRSK EGTGLGLGIS QRFVQLMGGE
ISVTSKLGQG SCFSFSIPVS LTKAIPNSSS FPVDHAISIV PGQHYRIMIA EDNATNRLLL
SKILIRLGFE VKEAENGQIA IALWQQWQPH LTFMDMHMPI IDGYQATQRI RQLEQELATE
QSFTPTKIIA LTASAFTEQR QESLDAGCDD FVSKPFRWEE ILEILSKYLQ IEYLYESTSD
SDITLNTISF SSEYVLDQKA LAIMPAEWIH ELHFAAVQGN DMSSLHLIAQ IPPEQTSLIA
ALTGLIESYQ FDKLMLLTQP KE
//
