ID M2Q1B8_9FIRM Unreviewed; 610 AA.
AC M2Q1B8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMD16061.1};
GN ORFNames=HMPREF9943_01464 {ECO:0000313|EMBL:EMD16061.1};
OS Eggerthia catenaformis OT 569 = DSM 20559.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Eggerthia.
OX NCBI_TaxID=999415 {ECO:0000313|EMBL:EMD16061.1, ECO:0000313|Proteomes:UP000011758};
RN [1] {ECO:0000313|EMBL:EMD16061.1, ECO:0000313|Proteomes:UP000011758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT 569 {ECO:0000313|EMBL:EMD16061.1,
RC ECO:0000313|Proteomes:UP000011758};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Mathney J., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lactobacillus catenaformis F0143.";
RL Submitted (FEB-2013) 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:EMD16061.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGEJ01000024; EMD16061.1; -; Genomic_DNA.
DR RefSeq; WP_004803589.1; NZ_KB446649.1.
DR AlphaFoldDB; M2Q1B8; -.
DR STRING; 999415.HMPREF9943_01464; -.
DR PATRIC; fig|999415.3.peg.1491; -.
DR eggNOG; COG0515; Bacteria.
DR OrthoDB; 9788659at2; -.
DR BioCyc; ECAT999415-HMP:GTTI-1508-MONOMER; -.
DR Proteomes; UP000011758; 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 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; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 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; 2.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000011758};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 364..432
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 498..575
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 577..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..610
FT /note="Polar 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 610 AA; 67740 MW; AC2BE1DFB749A28C CRC64;
MSEVNRILAG RYLLQRLIGQ GGMADVYLGE DTILKRIVAV KILRSSLTGD PIYITRFHRE
ASAAAALSHP NIVAIYDVGD EDDLYYIIME YIRGQTLKSL IHKRGALHYV EAIDIMKQVA
SGVAHAHSNG IVHRDLKPQN ILVTDSGTVK IADFGIASIQ SLSQVTQTDT IMGSLHYLAP
EIARGEKATP QSDIYALGIV FYELLRGEVP FNGESPVNIA LKHMRDEIPS VRSFNPSIPQ
SVENIIIKAT AKNIKDRYHD ANEMLQDLMT CLTRENESKI VFDIIDDDPT IVAGETQFFK
KEEIEEKKVP VEKEPLENRT SRVTRIDQKQ KRSLNIPKKK IAIAVSVILA VCLLIGVIVF
INNSSQTAKI PDVTGLKKSE AISLLKEKGY KIDKTEDSEL SDKYEKNYVI QTTPKVGTIV
AKNSLIRLTV SSGKYIVMED YTGKKYNNVK AKLEALGFKV KKYEKSDEEY ASGIVIDQSI
SAGEKQDPNT KNKTITLTVS KGITITVPYL YGENIESAKK TLKNLGFNPT AEVLSPPTDK
NEASKITINT VVKMSLDPYT QVHEKNKKII IYYYDRKPET NNDNSNNGGT NTDGNTNNQG
RSNNNGGTGH
//
