ID A0A1I1LQG5_9CLOT Unreviewed; 638 AA.
AC A0A1I1LQG5;
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:SFC72543.1};
GN ORFNames=SAMN05421842_10857 {ECO:0000313|EMBL:SFC72543.1};
OS Clostridium uliginosum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=119641 {ECO:0000313|EMBL:SFC72543.1, ECO:0000313|Proteomes:UP000199263};
RN [1] {ECO:0000313|EMBL:SFC72543.1, ECO:0000313|Proteomes:UP000199263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12992 {ECO:0000313|EMBL:SFC72543.1,
RC ECO:0000313|Proteomes:UP000199263};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FOMG01000008; SFC72543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1LQG5; -.
DR STRING; 119641.SAMN05421842_10857; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000199263; 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 GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
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; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
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:SFC72543.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000199263};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SFC72543.1};
KW Transferase {ECO:0000313|EMBL:SFC72543.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 342..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 369..434
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 435..502
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 503..572
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 298..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 638 AA; 69427 MW; DB659A8B92FD9397 CRC64;
MNGIILGNRY ELLEKIGEGG MSEVFKARCN KLNRLVAVKI LKKEFCNNSE IVQKFKGEAT
AIATLSDNNI VNILDVGTQE DINYIVMELV QGKTLKDVIN SSGKMNYEIA ISTAIQIAKA
LDCAHRNKII HRDVKPQNIL VSENGAIKVT DFGIAKSTSS ATITNTSTIM GSAHYLSPEQ
AKGSFIDCRT DLYSLGVVLY EMVTGALPFE ADTAVTIALK HLQEEAVSPK SLNSKIPDSL
NKLILKCMEK DPNKRYQSAK EVIKDLQKIK ENPNAIIDKV VDDQHTIIMS AVTEEISKQS
SKKDSKNEES EFYDDDYDDE EYDYDDEEAP KKSVNNKKAM KLIIAIGGVV LLIALVVGIV
TFFSATGIGK EVEIPDIVGS TIEDAKTKLT NIDLVLVEAG TDKSDKPEGT ILEIDPKAGT
KVKTKSKVRV IVSSGETKLK MPDLREDDLD TAKKKLESLK LKIDSSTEEY NDDISKGQII
KQQPNADAEI TTSTKITVVV SKGPQIRLST VPNVTGLSSD EAKTGLEKAR LRVSTVEKVT
ENEAEDGKVL AQSIDGNSKV EQGTTVNITV GKYVKPKENP VVKPEETPGT TTPNTPGGTT
PNTPGTTPPT NPNEPTPPVD SNNKDKPVQG QITPKKPQ
//
