ID A0A086Z2L5_9BIFI Unreviewed; 759 AA.
AC A0A086Z2L5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:KFI40765.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:KFI40765.1};
GN ORFNames=BACT_1472 {ECO:0000313|EMBL:KFI40765.1};
OS Bifidobacterium actinocoloniiforme DSM 22766.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI40765.1, ECO:0000313|Proteomes:UP000029015};
RN [1] {ECO:0000313|EMBL:KFI40765.1, ECO:0000313|Proteomes:UP000029015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI40765.1,
RC ECO:0000313|Proteomes:UP000029015};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:KFI40765.1}.
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DR EMBL; JGYK01000001; KFI40765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086Z2L5; -.
DR STRING; 1437605.AB656_05660; -.
DR eggNOG; COG0515; Bacteria.
DR Proteomes; UP000029015; 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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:KFI40765.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029015};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KFI40765.1};
KW Transferase {ECO:0000313|EMBL:KFI40765.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 635..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 288..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 759 AA; 78395 MW; 5B67C15B8CDF00AA CRC64;
MDVLNLQTGD EVGGYTLIAP LGGGAMGSVW RVQDDGGTDY AMKVLRDSLA EKDGQADGQG
GTDRASARER LRREAMSLRR IDHPGVCRIV DMELDDSLAF IVTELIEGLN LSDDVSTNGA
YSGDDLERLA AKLIDAVAAV HRAGIVHRDI KPTNVMISAA GPVLVDFGIA MGAGEAHVTR
TGLVMGTPGF IAPEVIDGAE SDEESDWWST AAVLAYAACG KPVFGSQPMM AVLERAASGS
ADLTGLPART MAAFRAALSP RRQDRPRPQA LLDAIGLDAL QPELWERDDE PDDQQDSEQG
EDSGESGQSQ PGDEESEGVV RPFGASSSTD RRPGPSGGAQ ASGVGDARNL TAGETTQVLG
GPASNPRLTW RTQNVDTART QALADSGPED ATTLAGLTRT LPAKESELGA TADWDEAEDG
AEDDAEKTWV GGPSSATRTL PAMTTALPAE VGGPSLQAGT MAQAAPRIAP EAAVPGQYAA
PATPYGPYAQ APLDPPAAVR WRERYKRGRP VLWMIGLLAA ALAALTPFSA CLLSSLALWA
LATAGLSLGG QMSRELKRGD GRRRRDALLN LASLPWLAIK ALAMTLPRLL ILLTTDALGL
AAGGWLLGTP KVSGKLGLFG AVIPLPLVAG KSSSAAGLLA ATCALVGWLL AAFAGGGGGA
SNSATAPGTK DWRLAVRLGA GALPGKGAQE REAEQAQQAA AAGLSGQADP LQGTPAQASR
RRPLILLALW VLILGVLLAF IASGTTLDWA PITLMPASS
//
