ID A8RCM7_9FIRM Unreviewed; 552 AA.
AC A8RCM7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Serine/threonine-protein kinase PrkC {ECO:0000313|EMBL:EDP10849.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:EDP10849.1};
GN Name=prkC {ECO:0000313|EMBL:EDP10849.1};
GN ORFNames=EUBDOL_01448 {ECO:0000313|EMBL:EDP10849.1};
OS Amedibacillus dolichus DSM 3991.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Amedibacillus.
OX NCBI_TaxID=428127 {ECO:0000313|EMBL:EDP10849.1, ECO:0000313|Proteomes:UP000004090};
RN [1] {ECO:0000313|EMBL:EDP10849.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10849.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium dolichum (DSM 3991).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDP10849.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10849.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2007) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP10849.1}.
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DR EMBL; ABAW02000021; EDP10849.1; -; Genomic_DNA.
DR RefSeq; WP_004799855.1; NZ_DS483476.1.
DR AlphaFoldDB; A8RCM7; -.
DR STRING; 428127.EUBDOL_01448; -.
DR GeneID; 83060196; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR Proteomes; UP000004090; Unassembled WGS sequence.
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 GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd06577; PASTA_pknB; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
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; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF03793; PASTA; 1.
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; 1.
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:EDP10849.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:EDP10849.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 335..405
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 552 AA; 61889 MW; 5EE14053DE6F4F29 CRC64;
MDKMIAERYM LVSLLGEGGM ADVYLAIDTI LNREVAIKIL RGELSKDPVT LLRFQREASA
VSKLNHPNVV DVYDVGEYEG KHYIVMEYIR GRTLKQLISQ RGALHKEEAV NIMKQLTSAV
EHAHENHIIH RDIKPQNILV KDDGTIKITD FGIALAHDAV QLTQNDAVLG SAHYLAPETT
RGEAPTVQVD IYALGIVFYE LLTGSVPFKG DNPVQIAMKH LREEIPSVCE FNPTLPQAVE
NIILRATVKN REQRYHSAKE MLYDLECCLK PEYAHVDKLK FTAEDDPTRI MHKETAESSS
LEEEKTKRLN KTIVIAVSLI CVVIAAVLLW FAFGHEKSIM IPNITTAQTK QEAIKTLTES
GFEEENIEIK EELSDNIEKG YVIKVSPKVG EKARVSQTIT LSISRGTYFV MKDYRNEELA
QVEAELKAAM PKLKLHVTKE QRSGILPGRI LAQSGIDIGE KLDPEKEYTL NVTVSEHMQY
VIEGIIGLPY QEAVALIEEK TGVKPVLEQL DASDLSEEEK AKIKPGVVVE VDPKEGTAYT
QDGESVITIR FY
//
