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Database: UniProt
Entry: A0A1Z4GY40_9CYAN
LinkDB: A0A1Z4GY40_9CYAN
Original site: A0A1Z4GY40_9CYAN 
ID   A0A1Z4GY40_9CYAN        Unreviewed;      1862 AA.
AC   A0A1Z4GY40;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-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=NIES2100_21530 {ECO:0000313|EMBL:BAY22390.1};
OS   Calothrix sp. NIES-2100.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1954172 {ECO:0000313|EMBL:BAY22390.1, ECO:0000313|Proteomes:UP000218319};
RN   [1] {ECO:0000313|EMBL:BAY22390.1, ECO:0000313|Proteomes:UP000218319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2100 {ECO:0000313|EMBL:BAY22390.1,
RC   ECO:0000313|Proteomes:UP000218319};
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 + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; AP018178; BAY22390.1; -; Genomic_DNA.
DR   OrthoDB; 573511at2; -.
DR   Proteomes; UP000218319; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAY22390.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:BAY22390.1}.
FT   DOMAIN          11..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1604..1858
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1550..1595
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1862 AA;  209948 MW;  490DDC637D67C6E4 CRC64;
     MPTALLKITG YRIDEQIYAG NRTVVYRGIR EQDLQPVILK MMRNNSPTFS ELIQFRNQYT
     ISKNLDIPGI VQAYSLEEYG NGYVLVMEDY GGTSLSSYLN QYTNSGKFTL DEFFPIAIAI
     TATLGELHRK RIIYKDVKPA NILIHPQTKQ VKLIDFSIAS LLPRETQQLQ NPHVLEGTLA
     YISPEQTGRM NRGIDYRTDF YSLGVTFYEL LTGKLPFESS DPIELVYCHI AKQPNQVNSQ
     NIPQVLGDIV LKLMAKNAED RYQSAAGLKS DLELCFCEWQ EQRAILPFQL AQKDISDRFL
     IPEKLYGRQK EVETLLTVFD RVAGNKEQIN QPSELLNRSE LILITGFSGI GKTAVVNEVQ
     KPIVRQRGYF ITGKFDQFQR NIPFSAFVQA LQDLMAQILT ESDAQITQWQ QKILAALGDN
     AQVIIDVIPE LKKIIGTQPP VTELVGNAAQ KRFNRFFRKF IQVFTTPEHP LVIFLDDLQW
     ADTASLKLVQ MLMSERQIRH LLLIGAYRNN EVSHTHPLML TLEQIRTSQH PKAITTINLA
     PLTATDINHL FTDTLSCKLE EALPLTQIIY PKTQGNPFFT IQILKTLHTD GHINFASEIG
     SWQYDLNQVQ TLNLTDNVVE FMILQLQKLP KATQDVLKLA ACIGNTFDLA TLAIVYEKSL
     TQTASDLWSA LAEGLIMPTS QTYKLFQQKN EQIKPEDELA AEDSSLYLTE TEVHFVAHLQ
     HWSAYPAEDN HFPSQDYIYE FLHDRVQQAA YFLIDEAQKQ ITHLQIGKLL LQNIPIAEQE
     EQIFEIVNHL NMGLQLLTAP QEREKVAQLN LQAGRKAKAS TAYATASQYL AIAMQLLAED
     SWLQQYKLTF DIYKERSEVE YLNSNFEQSY ILIQKALTQA QSAVEKAALY KLLIVQHTLQ
     ADYAVAIQVG KQALSLLGIN LPEENIKSVI DAEIKAIKAS LENQKISAIL ELPENPNPIY
     RYAIQLLIDL DPPTYITSAI DLYILVTLKA VNLSIQYGNV AESAKAYVNY GFLLGSVFGD
     YQTGYEFGVV ATQLAEKFHH KGQKCQVDLL LGSWLHNWIK PTHLAIPINN AGYQAGLESG
     ELQFAGYNLF GNICNQYFQG INLNNIRLDI CKFLPFAHQT QNTLLTEMLL EVQKVIDSLM
     GYCNYQDSVE CRHVSQTPMA LAIAHILQAQ LAYLQAQYQL ALQYIIQAEA YLPAILGFTT
     SASYPFYHAL ILAALYPQVP PSTQEQYWQS LITHQNQLQI WAKNCPENFE HQYLLIQAEM
     ARISKQEFEA MDLYDRAIAS AKANGFTQNL ALANELAVKF WLGKNKTNIA QLYLTGAVSA
     YTQWGATAQV KYLQAHYPEL LPPHKALSPK ELEYDQQSTI STSNINFSAQ LDLAAFLKAS
     QAIAGEIQLD QLLSILMQVM LENAGAKKSV LLLCKNNQLA YAAIAGLDEG KIFSHTNVSA
     IQPEESQDIP LTVINYVKRT LEPLVIDDIV TQSRFIHDPY IIKNQPRSVL CTPIINQGEL
     IGLLYLENQL TSGVFTRDRL EVVQLLTAQA AISLKNAQLY TDLSTTTASL KQANSQLAEY
     SHTLEAKVAE RTAQLEEAFK NLQTAQAQLI QNEKMSSLGQ LVAGIAHEIN NPISFIYGNL
     TPANEYIDDL MFVLQSYRQH YPHPTPQLQA QIAHIELDFI TKDLPKILNS MQVGAERIRD
     IVMSLRNFSR LDEAEIKAVD IHEGIDSALM ILQNRLLANP ERPEICVIKE YSQLPAIKCY
     AGQLNQVFLN LLMNAIDALE ESIRRGKILA QLQIYIRTQI CDSEQIKIAI ADNGMGISDS
     HKPYVFDPFF TTKQVGQGTG LGLSISYQII VDKHQGQLEC QSIPGEGAEF IITLPIRRIT
     NS
//
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