ID L8MYF5_9CYAN Unreviewed; 422 AA.
AC L8MYF5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Pse7429DRAFT_1638 {ECO:0000313|EMBL:ELS33042.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS33042.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS33042.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS33042.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS33042.1}.
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DR EMBL; ALWB01000061; ELS33042.1; -; Genomic_DNA.
DR RefSeq; WP_009626816.1; NZ_ALWB01000061.1.
DR AlphaFoldDB; L8MYF5; -.
DR PATRIC; fig|927668.3.peg.2085; -.
DR OrthoDB; 9773246at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19920; REC_PA4781-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELS33042.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ELS33042.1}.
FT DOMAIN 9..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 167..422
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 422 AA; 46823 MW; A20C4D929E26BA74 CRC64;
MNVEDSNTLI LIVDDTPTNL DVISEALSDA GYDVAIATSG ERALHQVERK LPDLILLDVM
MPEIDGFETC RRLKSNPKTT NIPIIFMTAL SDMSNKVKGF ELGAVDYITK PFQEQEVLAR
VRTHLQLSLL TQKLEDQVMQ KTAALQASQL QIIQSEKLSA LGNLVAGVAH EINNPIGFLG
GNIQPALGYI KDLFSLLDLY QKKYPDPDPD IQEEIDNIDL AYIREDLPKL VGSMREGIKR
IKDISNSLRT FSRADSDAKQ TFNIHEGLDS TILILRHRLK ANEQRPEIEV VTEYGQILPI
KCFPGQLNQV FMNILANAID ALDEASQKRS YAELQANPNR ITIQTSESEK HVKIKITDNG
KGMSAEVKNK IFDHLFTTKA VGKGTGLGLA IAKQIVVEKH EGSIEVNSII GQGSEFLILL
PL
//
