ID K9UUA3_9CYAN Unreviewed; 860 AA.
AC K9UUA3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AFY99135.1};
GN ORFNames=Cal6303_0024 {ECO:0000313|EMBL:AFY99135.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFY99135.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFY99135.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFY99135.1,
RC ECO:0000313|Proteomes:UP000010477};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the leucine-binding protein family.
CC {ECO:0000256|ARBA:ARBA00010062}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003610; AFY99135.1; -; Genomic_DNA.
DR AlphaFoldDB; K9UUA3; -.
DR STRING; 1170562.Cal6303_0024; -.
DR KEGG; calt:Cal6303_0024; -.
DR PATRIC; fig|1170562.3.peg.29; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG0683; Bacteria.
DR HOGENOM; CLU_016565_0_0_3; -.
DR OrthoDB; 446586at2; -.
DR Proteomes; UP000010477; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06268; PBP1_ABC_transporter_LIVBP-like; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028081; Leu-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF13458; Peripla_BP_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:AFY99135.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AFY99135.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:AFY99135.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..337
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 860 AA; 96586 MW; 3CD801D12FA73AD7 CRC64;
MRVYCTRPCG DEPHINDIDE KYLTHGSTPQ RYCSTCGMPL ILKNQYLPLQ ELGSGGFGRT
FIVLDLNAPG EILGEKKRRI VKQLYPRTSL SQDEIKLVEN LFRKEAEVLE ELKHPQIPQL
YAFFELSIPQ YIPNSNQVPL EEQQKLFYLV QEYIEGDDLS QELQKRKDAG VSFFNEAEVA
QVLLEILDIL KFIHSHHKKI IIHRDIKPNN IIRHQQTKKL YLIDFGAVKQ VIQKVENQAD
KTENIIVTRG FSPPEQEAGT RVSFSSDLYS LAATCVNLLT GENPKTLGIP YDLNSWQNRV
KVKPALTRIL NKMLAANAKN RYQSADDVIK ALKMAGLIPS KTSYGNLPIW LLALGGGGII
GAIALCLYWL YSTIFPPPTP IIEPLAVNYF SRGEESITTQ VSTVPQCQPG YQAKAAGMEA
FQQKKYQIAE KKFQEAIKLF ADTRKNNSKS ECSGDPETII FLNNAKANLA GNPLTLFLAT
TSGKVENDSV TMEMLRGIAQ AQDKINSNQG IKGQLVEVIL GKDDENSEIT KRMAQHIIEN
NIPGEEESRI NIIGAIGHYT SDITLISGNV LGNTKYQDNR VPLISPSSSA VRKTQNIQVK
HAINLNDYVF RVVPNDRFTA EKLAGYVRDK LNLQRVLVVF NSRDKFSISL KEEFIMRMKN
KGVQATDIIE CNLKEKQPRQ CIALAKSNKS QVLMLATPAE GEVWAVINAN RNNQLNLQLI
GGDTVYSQVV LNETGEASEG MVVPVYVNLK SAKNKSNENF KLFEKKSQEF WGTTDVSWRT
ISTYDAMETL VTALQQLSKQ GKPLTRLNVY ETLKNPNFVA QGATAIVKFQ ERDRIPVPGL
SVLFQVKRNT EGNLKFEPIE
//
