SPKB_SYNY3
ID SPKB_SYNY3 Reviewed; 574 AA.
AC P74297;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine/threonine-protein kinase B;
DE EC=2.7.11.1;
GN Name=spkB; OrderedLocusNames=slr1697;
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 CHARACTERIZATION.
RX PubMed=12732981; DOI=10.1007/s00284-002-3887-2;
RA Kamei A., Yoshihara S., Yuasa T., Geng X., Ikeuchi M.;
RT "Biochemical and functional characterization of a eukaryotic-type protein
RT kinase, SpkB, in the cyanobacterium, Synechocystis sp. PCC 6803.";
RL Curr. Microbiol. 46:296-301(2003).
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: Protein kinase required for cell motility, but not for
CC phototaxis.
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 -!- 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;
CC -!- PTM: Autophosphorylated.
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; AB046598; BAB17034.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18391.1; -; Genomic_DNA.
DR PIR; S76132; S76132.
DR AlphaFoldDB; P74297; -.
DR SMR; P74297; -.
DR IntAct; P74297; 4.
DR STRING; 1148.1653478; -.
DR PaxDb; P74297; -.
DR EnsemblBacteria; BAA18391; BAA18391; BAA18391.
DR KEGG; syn:slr1697; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1357; Bacteria.
DR InParanoid; P74297; -.
DR OMA; MAMRPVY; -.
DR PhylomeDB; P74297; -.
DR BRENDA; 2.7.11.1; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR001646; 5peptide_repeat.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016252; Ser/Thr_kinase_SpkB.
DR Pfam; PF00805; Pentapeptide; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000647; Ser/Thr_PK_SpkB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..574
FT /note="Serine/threonine-protein kinase B"
FT /id="PRO_0000171240"
FT DOMAIN 34..301
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 454..493
FT /note="Pentapeptide repeat 1"
FT DOMAIN 504..543
FT /note="Pentapeptide repeat 2"
FT REGION 319..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 574 AA; 63079 MW; D96B2C5ABEE405A3 CRC64;
MSFCVNPNCP HPKNPNNVQV CQACGNSLRL NGRYQTLGLL GKGGFGATFA AADVALPGTP
ICVVKQLRPQ TDDPNVFRMA KELFEREAQT LGRVGNHPQV PRLLDYFEDD HQFYLVQEYV
KGHNLHQEVK KNGTFTEGSV KQFLTEILPI LDYIHSQKVI HRDIKPANLI RRQTDQKLVL
IDFGAVKNQI DSVLSSNTSA QTALTAFAVG TAGFAPPEQM AMRPVYASDI YATGVTCLYL
LTGKTPKEID CNSQTGEMDW EKHVTVSSKF AEVIRKMLEL SVRHRYKSAQ QVLDALEMPT
YEDGMMQGMV STPFTTLTGA GDEPATGIRM GNSSSPDYGD PSTRFNTNVQ PRDPSSTSLN
TGIKTRTAKP RQSPRDRATS NIESPTTRVR PASNMADGGS VGAGGIDYNM VNPKPFSRRE
EEKQAIANQP ETKRWNGKTF LAEYAQGKRD FADQNLVGIV LAKAFVPGIN CYQANLTNAN
FEQAELTRAD FGKARLKNVI FKGANLSDAY FGYADLRGAD LRGANLNGVN FKYANLQGAN
FSGADLGSAK VSPEQLKLAK TNWRTVMPGS GRRR
