ID A0A0D6L109_9CYAN Unreviewed; 2003 AA.
AC A0A0D6L109;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FDUTEX481_01608 {ECO:0000313|EMBL:EKF05436.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF05436.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF05436.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF05436.1}.
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DR EMBL; AGCR01000005; EKF05436.1; -; Genomic_DNA.
DR RefSeq; WP_045868416.1; NZ_JH930357.1.
DR STRING; 1188.FDUTEX481_01608; -.
DR PATRIC; fig|1188.3.peg.1612; -.
DR HOGENOM; CLU_000445_34_2_3; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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; 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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 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; 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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKF05436.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1547..1763
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1787..1903
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1836
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2003 AA; 226815 MW; 00DB3103A8BE0C53 CRC64;
MSITIAGYNL IEVLYDGTTT CVYRALRETE QTSVIIKTLK AEYPTRQQLT QLRHEYQILQ
NLNIAGIVKP LALENYHNGL ALILTDFAGE TLNNFINIQN FDLSKFLNIA IQLATILADL
HQNNIIHKDI KPQNILINPQ IDKVEIIDFS ISSYLFSETQ NPSDTNFLEG TLAYMSPEQT
GRMNRAIDYR TDFYSLGVTF YEMLTGQLPF QVNDSLELVH CHIAKTPVSP QEIHSAIPPV
VADIVMKLLA KTAEDRYQNA LGLKADLEEC LRQLQATGKI SHFQIGQLDL SSQFLIPQKL
YGREVEVMML INAFERVSLG ATEMMLVSGY SGIGKSCLVN EVHKPIVRQR GYFISGKFDQ
FKRNIPYASL IQAFQELIRQ LLTESSEQIA NWQAKLLAAL GNNGQIIIDV IPDVERIIGT
QPEVPQLGPT ESQNRFNRLF QQFIHVFCQP EYPLVVFLDD LQWADSASLK LIQLLTNNPD
SQYLLLIGAY RNNEVNETHP LILFLEAIQK AGAVINNILL QPLAISHVTQ LLSDTLHNHS
ENLATLADLL FNKTQGNPFF LTQLLKSLYQ ENLLSFNFTA RSWQWNIHLL QKIDITDNVI
ELMVSQIQKL LPNTQNILKL AACIGDKFSL EVLATVNKQN QSATVTDLWE ALQAGLILPL
NHASRIPLQL EQKEINNSEP TITYKFLHDR VQQAAYSLIT DEQKKATHLK IGQLLLQNAT
PEERKENIFA LVNQLNYGTE LLTSDSEKYE LAQLNFLAGQ KAKAATAYDS AVRYFNVGLK
LLPVNSWYQQ YEITLALHQE TAEAVFLIGD FEQMEQLIQV VLQQAKSQLH KVKVYELRIK
SCEVQRKLLE AVKLGLEAVE ILGVKLPESP TPFDVQQAIA ETTANLTTQE IEDLVNLPLM
TDAEKLAAFR LIVSLVPAAY QSAPTLFILM ACQQVNLSIK HGITSFSVSG FADYGILFSG
ILQDIEAADK FGQVALNLLD KLDTHEVRSK TLFKVATFIL PWKHHVRETL PLLENAYHSG
LEYGDLIHAG YAASNKCQYA YWSGYELKSL EQEMARYSQA IAQINQETAL NWHQIFHQAV
LNLIGESKNP CLLVGTAYDE EEFLPVHIQF NERTVIHYVF LNKLILCYLF GEFSQAVAHA
SQAQQYLDGV IGWLMVPLFH FYDSLAQLAI YSSLPQPQQQ ELLTRVINNQ QKMQKWAHSA
PMNHLHKFYL VEAERHRVLD EKIEAVEMYD RAIALAKDND YVNEEALAWE LAAKFYLSWG
RQTIARTYMS NAYHAYSRWG AIAKIKDLEI RYPQLITISP NTQNLEIHYQ ELNQANFPII
GRTQSLDLMT VMKASQALSC EIVLSKLLTN LMRILIENAG AEKGFLILEK AGKLQIEASG
SIEQEEISVE QSLPIENSQQ LPISIINYVQ RTQKDVVLND ATSEAVFNFD NYILNQKPKS
ILCTPIVNQG KLIGILYLEN NLTTGAFTPQ RLEVLQLLSS QAAISIENAR LYHDLAEYNR
TLEVRVEERT LELQGKNLQL QQEIRDRQRA EEVAETANRA KSQFLASMSH ELRTPLNGIL
GYTQILNKNQ TLTPEQKNGI KIIHQCGEHL LTLINDILDL SKIEAGKLEL YPTEFSLSEF
LESIVQICRI RSEQKGIALV FDQLSVLPKV VRADEKRLRQ VLINLLSNAV KFTEKGTVRF
QVGYHAEKFR FQVEDTGIGI AEEQLEEIFL PFKQVGEDSR KTEGTGLGLA ISRQLVEMMG
GELKVTSTLG KGSVFWVDLD LAEVAYPTNI KKIVERHITG FVSDQKKILV VDDKCSNRSV
LVNLLQPLGF EVLEATDGLD CLNKVLEFQP ALIFMDLVMT VMDGFEATRR LRMLPNFKEV
VVIAISASVF EFEQKQSLEV GCNDFLPKPF RVAELLEKLR IHLGLEWIYE DLETAQTQQK
NVNVKTKNQN LQLIPPPAEE IAILLDLAMK GDLRSIAQRA AKLEGLDEQL LPFTNHLHQL
AKEFKGKQIV DFIKQYSPVI GSK
//
