ID A0A1Q9JM92_9FIRM Unreviewed; 687 AA.
AC A0A1Q9JM92;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=BIV20_08785 {ECO:0000313|EMBL:OLR57342.1};
OS Roseburia sp. 499.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1261634 {ECO:0000313|EMBL:OLR57342.1, ECO:0000313|Proteomes:UP000186602};
RN [1] {ECO:0000313|EMBL:OLR57342.1, ECO:0000313|Proteomes:UP000186602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=499 {ECO:0000313|EMBL:OLR57342.1,
RC ECO:0000313|Proteomes:UP000186602};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR57342.1}.
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DR EMBL; MJID01000010; OLR57342.1; -; Genomic_DNA.
DR RefSeq; WP_075720653.1; NZ_MJID01000010.1.
DR AlphaFoldDB; A0A1Q9JM92; -.
DR STRING; 1261634.BIV20_08785; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000186602; 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-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:OLR57342.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000186602};
KW Transferase {ECO:0000313|EMBL:OLR57342.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 385..452
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 453..520
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 521..588
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 293..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="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 687 AA; 75345 MW; B87756B37FA979C8 CRC64;
MLKEGMYLAD RYEIVGKVGA GGMSDVYKAK DHTLGRFVAI KVLKQEFSED VNFVTKFRTE
AQSAAGLEHP NIVNIYDVGS ENGMYYIVME YVEGITLKTY IEKKGQLSFK EAVSIAIQVG
RGIEAAHNKH IIHRDIKPQN IIISTEGKVK VTDFGIARVA TTNTINADVM GSVHYASPEQ
ARNGFVDGKS DIYSLGIVMY EMVTGRVPFD GESTVAIAIQ HLQEEMVVPS AYAPNLPISM
EKIILKCTQK SPDRRYQTIS DLLMDLKKAL ISPDEDFVVM VPVGQQEKTR VMKPEELESI
KEQTGRVYYE EPDEDENEED DEDDEEEGGF LNPKMEKAVT IMGIVAAVII VLIVAYIAIS
LMGGMKFKSN DKDTDKDTDT KKEETADKVE MIDLTGMTFD EAKKALNEIG LGIKKGDSMS
SDKYEEGLIV GQSEKDGDMV EKNTTITVNL SSGAGEIEVP SVVGLDKDAA TDKLKSAGFN
NVKTEYEYSS DVPAGDVIRQ TPEGNAKAKK DDAITIYISR GTEQVKMINV LGMTEQQARD
ALAGINVSVS SVSSDYSDTV PEGSVISQSI SEGTFVNPGT SVTLTISLGK KVETYSLNNY
KIERLSEIPD NATGVSANIT LYKSEGNDKI NSWTATSFPF NISQGNIENC SSGYFVVDWS
WTVTDESGNV KNETKQTTIE GVNFTKN
//
