ID A0A2Z4U9A5_9FIRM Unreviewed; 737 AA.
AC A0A2Z4U9A5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Stk1 family PASTA domain-containing Ser/Thr kinase {ECO:0000313|EMBL:AWY97622.1};
GN Name=pknB {ECO:0000313|EMBL:AWY97622.1};
GN ORFNames=DQQ01_05030 {ECO:0000313|EMBL:AWY97622.1};
OS Blautia argi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1912897 {ECO:0000313|EMBL:AWY97622.1, ECO:0000313|Proteomes:UP000250003};
RN [1] {ECO:0000313|Proteomes:UP000250003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 15426 {ECO:0000313|Proteomes:UP000250003};
RA Chang Y.-H., Paek J., Shin Y.;
RT "Description of Blautia argi sp. nov., a new anaerobic isolated from dog
RT feces.";
RL Submitted (JUN-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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR EMBL; CP030280; AWY97622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4U9A5; -.
DR KEGG; blau:DQQ01_05030; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000250003; 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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AWY97622.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000250003};
KW Transferase {ECO:0000313|EMBL:AWY97622.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 366..390
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 413..480
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 487..553
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 556..624
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 302..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Basic and acidic residues"
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 737 AA; 79667 MW; 040293BC1EB526D3 CRC64;
MLNVGVIVGE RYEIVGRVGS GGMADVYKAK DHKLNRFVAM KVLKPEFSAD TNFIRKFQRE
AQAAAGLAHP NVVNVFDVGE DQGINYIVME LIEGITLKEY ISKKGRLTVK EATSIAIQVS
MGLEAAHNRN IVHRDIKPQN IIISTDGKVK VTDFGIARVA SSNTISTNAM GSVHYSSPEQ
VRGGYSDFKS DIYSLGITMY EMVTGRVPFD GDTTVAIAIK HLQDEMVAPS QYVPELPHSL
EEIILKCTQK SPDRRYSTLA ELINDLKHSL IDPNGSFVNL SPLSNHAQTI MITPEEMKQI
QNGAYSASSR YEEEDDDDDE DEDEEIYEKP SRKHRRKDED EDDEEDDDDD DERGGVNTKL
EKAMTIGGLI IGGVIICILI YMVASAAGLV KFGGKDKEDK KPQVQQEQQT DEAANKVAVP
DLTGKSEEQA GTELQALNLG KKKGGEEASD AVAEGMITRT EPAAGTQVDK NTTVVYYIST
GKAQEEDTNV TIPSGLVGQS LSHVQSTLQD LGLKTNVEKQ QSSSVEVGAV ISLNPGEGTS
VAKDTEVVIT VSTGEGNDMV SVANVRGIDA SEAEATLTAQ GLIVEIEEVD GDEVDVAYGE
VYAQTPKAGN RVEKGTTVTI KVRKEGAGSD AGTTADGNKV EAGQWAAVEP KLKKPDNYQG
GNVQLRLVQD DGDETSGGTV IMEGSPIDFD SNGGYYSVGS IVGKEGMESG TLYLAEQQEN
GEYQTLWSYP LTFTEVE
//
