ID A0A087BAM6_9BIFI Unreviewed; 696 AA.
AC A0A087BAM6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=BMAGN_0023 {ECO:0000313|EMBL:KFI68076.1};
OS Bifidobacterium magnum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1692 {ECO:0000313|EMBL:KFI68076.1, ECO:0000313|Proteomes:UP000029052};
RN [1] {ECO:0000313|EMBL:KFI68076.1, ECO:0000313|Proteomes:UP000029052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11591 {ECO:0000313|EMBL:KFI68076.1,
RC ECO:0000313|Proteomes:UP000029052};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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 -!- 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:KFI68076.1}.
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DR EMBL; JGZB01000004; KFI68076.1; -; Genomic_DNA.
DR RefSeq; WP_022860204.1; NZ_JGZB01000004.1.
DR AlphaFoldDB; A0A087BAM6; -.
DR STRING; 1692.BMAGN_0023; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR Proteomes; UP000029052; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
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; 4.
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:KFI68076.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029052};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KFI68076.1};
KW Transferase {ECO:0000313|EMBL:KFI68076.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 394..461
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 462..530
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 534..596
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 597..660
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 696 AA; 74034 MW; 46B57EA218089EFD CRC64;
MSSSNMPTQL DNGRYQLGQL IGRGGMAQVH VALDTRLGRT VAIKIMRTDF ANDEIFLARF
RREAHAVAQM NNPNIVNIYD SGEESILLEN GQTERVPYLV MEYVKGQTLR DIIKANGPLN
QRDAEYVMIG VLSALEYSHR MGIIHRDIKP GNIMISEQGV VKVMDFGIAR ALDDSATTMT
QSQGVVGTAQ YLSPEQARGE SVDMRSDIYS AGCVLYEMLT GRPPFTGDSA VAIAYQHVSE
VAPKPSSLVP GLSPMWDSIC GKAMAKDRQN RYATAAEFKQ DILTYMNGGM PVAAAFNPLS
DLTQNKNKRD AENAKNTVAY TSPVTNPGPP TQTFNPATGQ FEAIDPANTQ SRSQQRAAVV
KKRRKKHVIV ACIIIGVLLV AGLVGGFVWA QNNRVTMVTV PTFNESTTQA RAKQKLESVG
LVLEAKTDTN STLPEGTFTK QSPKGGSSVE EGSKVTVWFS AGPKSIKVPD VTGYSQSEAR
ETLTQAGFEV NDTVQTEDSS TIPKDSVTRT DPAANSMANK GSTIQLYVSS GMTKIPAGIV
GASKTDAVAK LQESGIAITI ESEYSDTVPE GTVIRVSPDS GTSVGQMSSA TIWVSNGPEP
VTVPSVIGMD TASAKSQLES AGFKVVVNGS SDSGARVTAM TPGAGESVKK GDTITLTSEK
PSSSSPSPSS SSSESDKNGD NGSSNSSSHA DQQNRP
//
