SPKE_SYNY3
ID SPKE_SYNY3 Reviewed; 614 AA.
AC P73515;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Serine/threonine-protein kinase-like protein E;
GN Name=spkE; OrderedLocusNames=slr1443;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LACK OF KINASE ACTIVITY.
RX PubMed=12168951; DOI=10.1093/dnares/9.3.71;
RA Kamei A., Yuasa T., Geng X., Ikeuchi M.;
RT "Biochemical examination of the potential eukaryotic-type protein kinase
RT genes in the complete genome of the unicellular Cyanobacterium
RT synechocystis sp. PCC 6803.";
RL DNA Res. 9:71-78(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Lacks protein kinase activity.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB046602; BAB17038.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17555.1; -; Genomic_DNA.
DR PIR; S77221; S77221.
DR AlphaFoldDB; P73515; -.
DR SMR; P73515; -.
DR IntAct; P73515; 4.
DR STRING; 1148.1652635; -.
DR PaxDb; P73515; -.
DR EnsemblBacteria; BAA17555; BAA17555; BAA17555.
DR KEGG; syn:slr1443; -.
DR eggNOG; COG0515; Bacteria.
DR InParanoid; P73515; -.
DR BRENDA; 2.7.11.1; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..614
FT /note="Serine/threonine-protein kinase-like protein E"
FT /id="PRO_0000171243"
FT DOMAIN 15..404
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 256..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 44
FT /note="Defective ATP-binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 614 AA; 68700 MW; 19B4F1DB691E96DB CRC64;
MTPSLSLGQR LDDRYLIQLH LGQNSLGQQY LAQDTHRFDE PCTITVLTAP PGDKAGNLFK
QQAEILYALD HPQIANFREF FALGSELYLV QDFIEGQSYF DLLKDRRLQG KAFTELEVRQ
WCRQLLPVLH YLHIQKICHG QISPSSIMRR TVDGLPVLVD FTHSQYYSGT PGEDRRDLHG
LGLGAIALLT GEVNPNPPWE NLLSSVALSQ EFRQLLLKLL AWPPLVDWPT LTDNLNNLPQ
HFLPTVAEFN LTSTIPEQTD NGVGKSSTGE PPFPTVHQSP ESSSSAKVKN MVRVDGLKGL
VKKSFILLGL MAIAMALGWG AGQLWLDNQQ RAALEKLAQE EPGDDVPEKT DLEIKNEIRA
RRLNLGISPQ RFQTLMDDGL AFQLGIDPQQ RLEKNPNTNG APLSLGSPEQ QMAMTITVLD
ALESLSREAT RDFAQNNSGD RRRWIPRVNQ LRLSSRSFYD LVNARFHHYL PMVSPALLGE
PEFEQRPLAQ VWNAMAFDSL ASLEDESHYQ RLSFDDTNQL NLNGTLEPGE GYAYAVTIPP
TEEFSLQLTA PPTARISFYP PTGPEVILQN SAMHRWSGPT DQAGYYELVI TSVAEEPIAF
ELELSIIPAS AQPF