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
//