ID K7RKI5_ACIA4 Unreviewed; 598 AA.
AC K7RKI5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=PACID_05680 {ECO:0000313|EMBL:AFV88409.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV88409.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV88409.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
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};
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; CP003493; AFV88409.1; -; Genomic_DNA.
DR AlphaFoldDB; K7RKI5; -.
DR STRING; 1171373.PACID_05680; -.
DR KEGG; pbo:PACID_05680; -.
DR PATRIC; fig|1171373.8.peg.573; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_11; -.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 2.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AFV88409.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:AFV88409.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 364..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 401..467
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 468..538
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 327..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 598 AA; 61565 MW; CFB2D1FEDFAC2AAC CRC64;
MTEAGSWLGG RYELLNVIGR GGMAEVWKAR DHRLGRDVAI KRLRADLASD ETFQARFQRE
AQSAAGLNHP NIVSVYDTGE GPDQNSGLSV PYIVMELVQG HTLRDVLRDD RKILPERALE
FTQGVLDALS YSHAAGIVHR DIKPANVMLT ETGQVKVMDF GIARAVSDTS ATMTQTAAVI
GTAQYLSPEQ ARGEVVDNRA DIYATGCLLY ELLVGRPPFL GDSPVSVAYQ HVREIPAPPS
SLDPEITPAM DAITLKALAK APADRYQTAK QMHDDIARVL AGQMPLAPLA TGAAAADEST
MATQVIAPAA ISGTAVRGTP VSPDSAGYAT GYGTTTSGLT PVAPGEGELD SQETKEPVKK
RKRWPIVLVV VLVVLALGVG GAGLYQAFGP GFGSSSTPTP TVKMVKVPAV TGMSQEGATS
TLANANLKAK VTTVRKDDAT AGQVIGQDPA RGRSVAEGST ITITVNQGPK KLTVPTGLEG
MSESAAKSAL TSAGFASGDI AVKYEESSTS DAGTVTGVSP SEGTEVDEGT SVTLTVASAP
APQPTITKTV EPTTAPTSTG GDTSTSQPTD TGGDGNGNGS GNGNGNGNGN NPTSGSTP
//
