ID A0A1I0EQG4_9FIRM Unreviewed; 649 AA.
AC A0A1I0EQG4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SET47536.1};
DE SubName: Full=Serine/threonine-protein kinase PrkC {ECO:0000313|EMBL:GFI41442.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:GFI41442.1};
GN Name=prkC_3 {ECO:0000313|EMBL:GFI41442.1};
GN ORFNames=IMSAGC017_01485 {ECO:0000313|EMBL:GFI41442.1},
GN SAMN04489758_11327 {ECO:0000313|EMBL:SET47536.1};
OS Thomasclavelia cocleata.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=69824 {ECO:0000313|EMBL:SET47536.1, ECO:0000313|Proteomes:UP000198558};
RN [1] {ECO:0000313|EMBL:SET47536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1551 {ECO:0000313|EMBL:SET47536.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000198558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1551 {ECO:0000313|Proteomes:UP000198558};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GFI41442.1, ECO:0000313|Proteomes:UP000490821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMSAGC_017 {ECO:0000313|EMBL:GFI41442.1};
RA Chijiiwa R., Hosokawa M., Kogawa M., Nishikawa Y., Ide K., Sakanashi C.,
RA Takahashi K., Takeyama H.;
RT "Single-cell genomics of uncultured bacteria reveals dietary fiber
RT responders in the mouse gut microbiota.";
RL Microbiome 8:0-5(2020).
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; BLMI01000177; GFI41442.1; -; Genomic_DNA.
DR EMBL; FOIN01000013; SET47536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0EQG4; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000198558; Unassembled WGS sequence.
DR Proteomes; UP000490821; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
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; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
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:SET47536.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198558};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SET47536.1};
KW Transferase {ECO:0000313|EMBL:GFI41442.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 361..429
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 430..497
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 562..640
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 649 AA; 72552 MW; 1C4E91AA0B8F89BB CRC64;
MSKIIAERYE LLELIGQGGM ADVYLAKDII LNRTIAIKIL RTSLAKDPIY VTRFQREASA
AAALSHKNIV EIYDVGEDED KYYIVMEYVP GRTLKELILK RGAVHVVEAI DIMKQVVSGI
AKAHQLGIIH RDLKPQNILV TDSGVAKIAD FGIASMQSLA QVTQTDVIMG SLHYLAPELA
RGEKATVQSD IYALGIVFYE LLRGEVPFNG ESPVNIALKH MQEDLPSLLE FNPSILQSVE
NIVIKATAKN LNDRYHNVTE MLEDLNTCME RPNEKKLEFV YDTETEPTIV LDSRSMFNSA
NTTNVASTTE SIQDDKVKDE KGLKKLLTKF KNLDIKAKVA IIVGVIFVAG VTTFLVYANI
RPDTNLMPDL EGKDKEQAIE LLKEYNVTIS DDIIEELSDE YEKGEIVKTD PKKGSTIKEG
DVVKLTISKG KYIVVDDYLG MDVDKAEKAL KKLGFKVIIE KEVSSKTKGT VIEQSIEKDE
KVDPTDKDRE ITLTVSKGNY TVISDYLGMD VEKAKEVLNN LGFKVYIDEK QSEKPQGTVI
EQSLQKGHKI DPDETDRTIT LTVSKGLEIE IPNVVGMEIN AAKSRLESKD FKVVLSKLST
DSLSDEEIER IEINRVMKQS PESFGTVNKK GETITLYYYD SKPDNSMND
//
