ID A0A1Y4NC07_9FIRM Unreviewed; 656 AA.
AC A0A1Y4NC07;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:OUP78344.1};
GN ORFNames=B5F09_02695 {ECO:0000313|EMBL:OUP78344.1};
OS Erysipelatoclostridium sp. An173.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=1965571 {ECO:0000313|EMBL:OUP78344.1, ECO:0000313|Proteomes:UP000196550};
RN [1] {ECO:0000313|Proteomes:UP000196550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An173 {ECO:0000313|Proteomes:UP000196550};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP78344.1}.
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DR EMBL; NFKR01000004; OUP78344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4NC07; -.
DR Proteomes; UP000196550; 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-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; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 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:OUP78344.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000196550};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OUP78344.1};
KW Transferase {ECO:0000313|EMBL:OUP78344.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 360..428
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 429..497
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 501..569
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 570..646
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 465..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 656 AA; 72376 MW; 72867198452DD2E8 CRC64;
MAKIIAERYE LLELIGQGGM ADVYLAQDII LNRTIAIKIL RTSLAKDPIY VTRFQREASA
AAALSHRNIV EIYDVGEDED KYYIVMEYVP GTTLKELILK RGAVHYIEAI DIMKQIVSGI
AKAHQLGIIH RDLKPQNILV TDSGVAKIAD FGIASMQSLA QVTQTDVIMG SLHYLAPELA
RGEKATAQSD VYALGIVFYE LLRGEVPFNG ESPVNIALKH MQEDLPSLLD FNPSIPQSVE
NIVIKATAKN LNDRYQSAAE MLDDINTCLD RPNEEKLVFS YDSDDEPTIV VDPRTAFSSN
DTSEVKTREE KPVEEEENDN FFKRFVKKIK GLSTRSKVII GAVTALVILG IAFVIYLNTG
SDANLMPDLA GRTVDEAREL LDDYGVTISD NIVEELSDEY DKGEIIETDP KAGTSIKEGD
VISLTVSSGK YIVLEDYVGM TQSEAEKAIA DLSDDVEIEV VIEEEVSSSP RGEVIDQDKD
SGTKLDPNDE SNLTITLTVS KGDYIVVGNY IGMSQSEAEA ALKKLGFTVT IETEESEEAK
GTVIDQSYNK GYRLDPDDDD RNITLTVSSG KTYQVRDVFD RNINSAKTIL ENNGFKVRLV
DLSNSTDQTL LSNYPFRSVN TVAGQSPEAD TTVNEQGTTV TLYYYSSQPE SANEED
//
