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Database: UniProt
Entry: K9VZE5_9CYAN
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ID   K9VZE5_9CYAN            Unreviewed;      2040 AA.
AC   K9VZE5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Cri9333_1993 {ECO:0000313|EMBL:AFZ12872.1};
OS   Crinalium epipsammum PCC 9333.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC   Crinalium.
OX   NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ12872.1, ECO:0000313|Proteomes:UP000010472};
RN   [1] {ECO:0000313|EMBL:AFZ12872.1, ECO:0000313|Proteomes:UP000010472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ12872.1,
RC   ECO:0000313|Proteomes:UP000010472};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL   Submitted (JUN-2012) 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; CP003620; AFZ12872.1; -; Genomic_DNA.
DR   RefSeq; WP_015202988.1; NC_019753.1.
DR   STRING; 1173022.Cri9333_1993; -.
DR   KEGG; cep:Cri9333_1993; -.
DR   PATRIC; fig|1173022.3.peg.2153; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   HOGENOM; CLU_000445_34_2_3; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000010472; Chromosome.
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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF01627; Hpt; 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; SM00073; HPT; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 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, ECO:0000313|EMBL:AFZ12872.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1520..1746
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1772..1889
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1944..2040
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         1821
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1983
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   2040 AA;  229472 MW;  E13EF715D250FE14 CRC64;
     MINIPGYQIK GQIYESQKKL IYQGKSDIDH KPVIIKVLKP GFFTAEEIAR LKQEYIISHD
     LNYLGIVKTY SIENYQNGFA LILEDFGGKS LRQVFTAKPM QLPEFLRIAI VLAETLIELH
     KIPIIHKDIK PANIIINPQT SEVKITDFSI ASRLGVENQV VSNPNLLEGT LAYMSPEQTG
     RMNRSVDYRT DFYSLGVTFY EMLTGELPFI HSDPMELVHS HIAKQPTTPA AIADIPQVIS
     DIVMKLLAKN AEDRYQSAAG LKFDLENCLQ QLQSKGKIDD FAVGKRDRSN QLLIPQKLYG
     RENEVQTLMD AFDLVSNGAS ELILVSGYSG IGKTSIVAEV HKPIVKARGY FISGKFDQFK
     RNIPYSALIQ AFQELISQVL TENAEQITVW RDKLLNALGE QGRVITEVIP KVELIIGQQP
     ELTPIGAFEA QNRFNRVFQQ FIQVFCQPNH PLVVFLDDLQ WADSASLKLI QLLVTNFDSK
     YLLMINAYRD NEVSSTHSFI QTLEKIKDTE ATINQIVVQP LSLYCVNQII AETLKTDPEA
     EQLKPLVSIV YNKTQGNPFY LTQLLKSLYS ENFLVYQVDN DTWHWDIQKI QAVGITDFNV
     VELLARSLRK LPPETQNILK LAACIGNQFN LDVLALVNQE SDTVTANHLW SALQCGLILP
     TSTAYKIPLV FQEEEAKYFH ANDVKVEYKF LHDRVQQSAY SLIPEAERKA THLKIGQQLL
     RNTTPESQNE NIFAIVNHLN FGIDLLNNQL DKNELAELNL IAGQKAKSAM AYEAAVNYLN
     LALNLLCPES WQEQYYLAFT IYKEAAEAEY LNASLDQAET LCNFALTQTQ VILDQIKFYL
     IKFKIHLAKN QINLALDLGL TILKMLGVPL SETPPSDINI EKLANLPRMT DPYKLAAMEI
     LMLLYSPATI SQSPLTLPFI YTMLALSSEY GNSPPSIYAY AIYGVITVWL IPDINLAYKL
     SQLSIQVLEK LNAKELYAKV YFTKEINISY KKEHLRETIK PLHECISNGL EVGDVEFSCN
     AANYYCNHLF FKGEVLDVVA QKQSEYIKYI QKLGQKHLLT ILKVFAQAVA NLLNSPRNPC
     LLTGEFMNET ETLPFFIGSN NLISIFNAYY FKCWLNFLFK EYKEAVKYGE LILTKCGAVK
     AEVIVVTQHN FYYSLALLSE YYRLKIKTNS SNQVDLEKYL EQVRKNQEKM KYWAEHCPEN
     FQHKYDLVEA EKAKVLGEKE KTIPSVSYAS ALYEQAIKGA KLQGYIQEEA LALELAGEFH
     LSCEHDRLGK YYLLEAYYCY VKWGAIAKAK HLEIQYPDLI PPSEKITKSK SFNTTLSSSS
     SADILDLTTV IKASQTIAGE IVLDKLLEKL MKIIIENAGA QTGFFILKNE FQAFIEARLV
     SEENQVIVRQ SPLSENTKLL PLSVINFVER TKEDVILINA SSSTQFNNDA YITENQPLSV
     LCTPIIHQNQ LLGILYLENN LITGVFTTER VGLLKILSAQ AAISLQNALL YRVAEQKAIL
     EKAKVAAEAA NQAKSEFLAM ISHEIRTPMN AIVGMSQLLL NTTLQPQQKA FVNTISTSSE
     SLLTILNDIL DLSKIESGKL ELEQQSFNLY RCIEESLALL TPKVIEKGLK LTYSIDPPTP
     ENLHGDSTRL RQVLLNLLSN AIKFTQTGGI NLAVTAEKLA RETNNESVYE IQFAIKDTGI
     GIPLDRIQQL FNPFTQVDAS ISRRYGGTGL GLAICKKLVE MMGGKISVES ELGHGSTFYF
     TIIATAASQE FALSTEESNG KIPHLAQEVP LKILLAEDNK VNQQVALLTF EALGYQIQIV
     NHGLEALQEL QQQNYDVVFM DIQMPEMDGI TATSYINQEW SSESRPQIIA MTAYVNKEDK
     ERCFQAGMDG YISKPIRIDE LVKVLKQCYL SINKNVAGCQ RLTSRQELEV SPSSSLLQQS
     QDTTLEVIDR YILQSLRQMA GANADEFLTK IINNYFEVAP QLLSEIDAAI DTADANKLFQ
     AAHALRSSSA NLGAAKLSGI CQELEAIGRS GTTVGAQSLR SQLKSMYQLV KDALLRECKD
//
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