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Database: UniProt
Entry: L8LT67_9CHRO
LinkDB: L8LT67_9CHRO
Original site: L8LT67_9CHRO 
ID   L8LT67_9CHRO            Unreviewed;       294 AA.
AC   L8LT67;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Chemotaxis protein histidine kinase-like protein {ECO:0000313|EMBL:ELR99977.1};
DE   Flags: Precursor;
GN   ORFNames=GLO73106DRAFT_00038310 {ECO:0000313|EMBL:ELR99977.1};
OS   Gloeocapsa sp. PCC 73106.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR99977.1, ECO:0000313|Proteomes:UP000011180};
RN   [1] {ECO:0000313|EMBL:ELR99977.1, ECO:0000313|Proteomes:UP000011180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR99977.1,
RC   ECO:0000313|Proteomes:UP000011180};
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   -!- 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:ELR99977.1}.
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DR   EMBL; ALVY01000085; ELR99977.1; -; Genomic_DNA.
DR   RefSeq; WP_006527202.1; NZ_ALVY01000085.1.
DR   AlphaFoldDB; L8LT67; -.
DR   STRING; 102232.GLO73106DRAFT_00038310; -.
DR   PATRIC; fig|102232.3.peg.264; -.
DR   eggNOG; COG2198; Bacteria.
DR   OrthoDB; 2079555at2; -.
DR   Proteomes; UP000011180; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ELR99977.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011180};
KW   Transferase {ECO:0000313|EMBL:ELR99977.1}.
FT   DOMAIN          2..109
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          96..123
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         49
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   294 AA;  32894 MW;  673099CB72B2072B CRC64;
     MDAATSDKIL GYFIEEAKEH LETLEKGILD LSTVVNDTER INELFRAAHS LKGGAAMLNL
     SSIQKTSHRL EDAFKILRDG EATVDQKLEE LFWDAYDVLQ DLIERLQSAL GLQEDEAEAI
     VKEAEPTFVE LQEYLQQQKV TATSSHATSG SYEQFSEAVI KELREMLNLF KQTPNPDNRH
     QLQQVCNNLQ QIAPDAQNWQ NLVGVAKVAI ANPKHSYELL APVIIKELKQ GGDYLELEQH
     ESIAPSLGLE RLAQARTPQV LLTVEPKAAA SVLLQVFDQV QVSELITLLQ NSHT
//
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