ID K9U9W7_CHAP6 Unreviewed; 686 AA.
AC K9U9W7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AFY91398.1};
GN ORFNames=Cha6605_0091 {ECO:0000313|EMBL:AFY91398.1};
OS Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC Chamaesiphon.
OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY91398.1, ECO:0000313|Proteomes:UP000010366};
RN [1] {ECO:0000313|EMBL:AFY91398.1, ECO:0000313|Proteomes:UP000010366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
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., 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 Chamaesiphon sp. PCC 6605.";
RL Submitted (MAY-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};
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DR EMBL; CP003600; AFY91398.1; -; Genomic_DNA.
DR RefSeq; WP_015157593.1; NC_019697.1.
DR AlphaFoldDB; K9U9W7; -.
DR STRING; 1173020.Cha6605_0091; -.
DR KEGG; cmp:Cha6605_0091; -.
DR PATRIC; fig|1173020.3.peg.99; -.
DR eggNOG; COG0226; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_375459_0_0_3; -.
DR OrthoDB; 428645at2; -.
DR Proteomes; UP000010366; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024370; PBP_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR30570; PERIPLASMIC PHOSPHATE BINDING COMPONENT OF PHOSPHATE ABC TRANSPORTER; 1.
DR PANTHER; PTHR30570:SF1; PHOSPHATE-BINDING PROTEIN PSTS; 1.
DR Pfam; PF12849; PBP_like_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFY91398.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010366};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AFY91398.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:AFY91398.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..294
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 686 AA; 75906 MW; 44C6954E49EB2743 CRC64;
MSLCINPQCM RSDNSDRMLF CQNCGSELLL AGKYRVAKLM SKKGGFGDTY EVTERGVPKV
LKVLKSNNTK AIELFDREYR VLESLAGEGI SGIPLVEDFF LYSPKDSQTA LHCLVMERIF
GMDLEEYIKV MKRPIDQKTA IGWLSQLTQI LQEIHQRGIF HRDIKPSNII LQPDGQLVAI
DFGAVKQAAV NTASGQKTRI FTPGYAAPEQ ELGETSAQSD FFSLGRTFVY LLTGKEPVEL
HDSYRNLLIW RDKTTNVSTD FSNLIDRLMQ DDPRQRPDTT ATIFREIAAL SPIITRQNIS
YQPPPPPTIS ERQQIQVANR APLAVPLAPH RLSPFKKLLP VLVVSTALLL LFSALAMYIL
GNRNSLVPGT SSKSTGESFT AIKDVPQGVF KFGGSTSWAT TRQLQSSIDA AIRGVYPQFD
IVYTDASSPD FKSTKNGKCS SNPGSNAGIC WLLEGDIDFA QSSISLEKSK YKDDDRVKTN
QLKQEAVAYD ALSVVVNPQL KLTGLTLDQL RDIYIGKVTN WSQVGGQNIP IVAFSRPENA
GGTVSSFKDL VLKKEDKLQF QTVSNTTEGL QQVAKNPGGI YFGAAKEVIV DYCSTKPLAI
GKTADNLVKP YQEPLKSVAD CNKGQRNKLE TKVIKTQEYP LTRQLYVIIK TTDPGRQKAG
EAYANLLKTK QGQSLLEKAG FVSIER
//
