ID K9PLL4_9CYAN Unreviewed; 1806 AA.
AC K9PLL4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cal7507_3279 {ECO:0000313|EMBL:AFY33684.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY33684.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY33684.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY33684.1,
RC ECO:0000313|Proteomes:UP000010390};
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., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003943; AFY33684.1; -; Genomic_DNA.
DR RefSeq; WP_015129493.1; NC_019682.1.
DR STRING; 99598.Cal7507_3279; -.
DR KEGG; calo:Cal7507_3279; -.
DR PATRIC; fig|99598.3.peg.3717; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_34_2_3; -.
DR OrthoDB; 573511at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 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; 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; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFY33684.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Transferase {ECO:0000313|EMBL:AFY33684.1}.
FT DOMAIN 11..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1546..1803
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1510..1537
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1806 AA; 203526 MW; 1D76D04F6D8F9379 CRC64;
MINALVKIPG YQVSEEIYNG SRTLVYRGYR EIDQKPVVIK LLKNFYPSFS ELLSFRNQYT
IAKNLNSPLI IQTYSLEPYQ NSYVLVMEDF GGISLKDYFT SVEALKITFL QEFLEIAIAL
CNALDILYRN CTIHKDIKPS NILINPETKQ VKLIDFSIAS LLPRETQEIQ NANTLEGTLA
YLSPEQTGRM NRGIDYRSDF YSLGVTFYEL LTGQLPFISD DPMELVHCHL AKTPILIHYI
IPEIPLILAE IISKLMAKNA EDRYQSALGI KHDLMICLHQ LQATGNIISF KLGERDISDR
FLIPEKLYGR EQEVKELLAA FERVSSGNSE MVLVAGFSGI GKTAVVNEIH KPIVKQRGYF
IKGKFDQFNR NIPFSAFVQA FRDLMGQMLT ESDAKIQLWK SKILEAVGEN GQVIVEVIPE
LERIIGTQEP APELSGSAAQ NRFNLLFQKF TQVLTTKEHP LVIFLDDLQW ADSASLKLMQ
LLMADTEHLF LIGAYRDNEI FPAHPLMLTL NAIQKTAATI NTITLEPLSQ FEVNELVADT
LKYKERLILN LSQLVYHKTQ GNPFFTTQFL KALHQDELIK FDFELGCWQC DIAQVTQQML
TSDVVEFMAL QLQKLPESTQ EILKLAACIG NQFDLATLAI VSEKSEIATA TDLWTALQEG
LILPQSDIYK YYQGEDKQQL RLENDPSKLL AKYKFLHDRV QQAAYFLIPD AQKQSTHLKI
GQLLLGNASA AEREEQIFAL VNQLNIGRSL ITQVAEREQL LQLNLTAAQK AKISTAYSAA
TQYLEICIEL LPEDSWQSQT DLTRTIYELA TEVAYLGTNY EQMEQLAAIF LSHTDSLIEK
IRVYEIKMLG AKAQGQLQES IQIGLQLLKL LGVEFPEQPT PADIGQALEQ TLVAWKNCSI
PSLLDLPVMT DPVTLAAMRI LTQMIAPAYQ SAPILMPLLI FKQINLCIAK GNCEISAFSY
ADYGLVLCGI VGDLDAGYQF GQLALNILSR FQAKTCKCRT YFIVHSYISH WKESLRSRLP
FFLEGYQVGL ETGDLESSSL NAQTYCASAY FAGYELPTLA AEMEIYRQGI LQLKQEIALN
YQGIYYQTVL NLLGASTEPW HLDGEVYAET QTLPTLQQSH NRTALYYLYY NKTVISYLFG
EYQRAADYTT LVDYYADSIV GMFAIPLFCF YSSLLDLKLY SSITETEQAK LLEKVAVNQE
KLKRWANHAP MNHLHKFSLV EAERHRVLGE KIEAIEMYDR AIALAKANEY IQEEALANEL
AAQFYLDWGK QKVAAGYMQE AYYCYAHWGA KAKTDDLEKR YPQLLQPILQ QQPINLRNDE
TIAFRATSSF TRTNSTSISD ALDFTSILKA AQAISSSIEL DEIIANLTQI ILENSGAKKA
ILILPQKGNW QVRAIISINY QPNSPDQTQT ILAQQSLDTY QDIPIKIINY VKNTKETVVI
DNCQTDIPGI IGEYMVEHQP KSVLCTPIIN QRHLVGILYL ENQITSGVFT NERLQVINLL
SSQAAISLEN ARLYQKSQQA LQDLQQAQLQ IVQSEKMSVL GNLVAGVAHE MNNPLGFIYA
SLKQAKPTIA DIVKHLKIYQ ESLPNKSEEI LQHAEEIDLD YSLEDLPKML DSMTMACDRL
NNISTSLRTF SRADKDYKVP FNIHEGIDST ILILKHRLKA NEQRPAIEVI SNYSNLPEIE
CFPGQLNQVF MNILANAIDA LEESNYGSSF EEIQANPNKI IITTSVEYNQ VKISIADNGK
GMSEEVKSKI FNHLFTTKAV GKGTGLGLAI ARQIIVEKHG GSLSVNSTLG QGTEFTILLP
VNGSAD
//
