ID A0A2Z4WBL7_9CLOT Unreviewed; 596 AA.
AC A0A2Z4WBL7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknB {ECO:0000313|EMBL:AWZ48718.1};
GN ORFNames=C3495_07785 {ECO:0000313|EMBL:AWZ48718.1};
OS Clostridiaceae bacterium 14S0207.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX NCBI_TaxID=2082193 {ECO:0000313|EMBL:AWZ48718.1, ECO:0000313|Proteomes:UP000250207};
RN [1] {ECO:0000313|EMBL:AWZ48718.1, ECO:0000313|Proteomes:UP000250207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14S0207 {ECO:0000313|EMBL:AWZ48718.1,
RC ECO:0000313|Proteomes:UP000250207};
RA Thomas P., Seyboldt C.;
RT "Complete genome sequence of Clostridium limosum strain from Germany.";
RL Submitted (FEB-2018) 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; CP026600; AWZ48718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4WBL7; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000250207; Chromosome.
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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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; 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:AWZ48718.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000250207};
KW Transferase {ECO:0000313|EMBL:AWZ48718.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 351..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 379..445
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 448..514
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 515..585
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 596 AA; 66818 MW; 9964DC783310F62E CRC64;
MKMIGSVLGN RYEIIEKIGE GGMSEVFKAK CRVLNRYVAI KVLKKEFSTD NEFVEKFKLE
ATAAAALSCN NIVSIYDVGS QDGINYIVME LVTGKTLKQV IRDRTRLSFN ETLDKGMQIA
RALECAHKNH IIHRDIKPQN ILVTEDGIVK VTDFGIAKAM NSATITNTTK IIGSAHYFSP
EQAKGSVVDF RTDIYSLGIV LYEMIVGKVP YDADSPVSVA LKHIQESVVP PIQLNPYIPE
SMNKLILKAM EKDPNKRYQT IKEMISDMQM IQFNQNTDIN VSSMDDTGDF TRIMDPITEE
QLGKTNIHTP VNNLDKVKNE DYDEDEDIEY LDDDVEDDKD QDKDERKKIK IIKWSIIALV
VLIVGIISTF SIKMIGLKGK KDVVVPTIIG LNKDEAKNKI EALGLNFVIE GEEENEKPKD
TIIKSNPSEG EKVKKDSDVK VIISKGKGKE IVLKNFVGIN FEEVKEMIKG EKLQVGNVTE
QYNDIVPKGQ VISQNPEPDT KVMENSSVDF VVSNGPESKS TRVPDLTNKT IQEAQTLLQG
ANLKLGNATT VPTPKKELDG KIINQSFEKN SEVKQGTYVN VTYYKFDLSL EFKNKK
//
