ID R8W5C1_9CLOT Unreviewed; 736 AA.
AC R8W5C1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=HMPREF1526_00447 {ECO:0000313|EMBL:EOQ39751.1};
OS Butyricicoccus pullicaecorum 1.2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Butyricicoccus.
OX NCBI_TaxID=1203606 {ECO:0000313|EMBL:EOQ39751.1, ECO:0000313|Proteomes:UP000013981};
RN [1] {ECO:0000313|EMBL:EOQ39751.1, ECO:0000313|Proteomes:UP000013981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1.2 {ECO:0000313|EMBL:EOQ39751.1,
RC ECO:0000313|Proteomes:UP000013981};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Van Immerseel F., Eeckhaut V.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Butyricicoccus pullicaecorum 1.2.";
RL Submitted (JAN-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:EOQ39751.1}.
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; AQOB01000002; EOQ39751.1; -; Genomic_DNA.
DR RefSeq; WP_016146654.1; NZ_KB976103.1.
DR AlphaFoldDB; R8W5C1; -.
DR PATRIC; fig|1203606.4.peg.418; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR Proteomes; UP000013981; 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; 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; 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:UP000013981};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 409..474
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 554..620
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 308..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 736 AA; 80841 MW; 5664B36DD0781B29 CRC64;
MDKYIGKLLD NRYEMLEILG VGGMAVVYKA RDRVLDRFVA IKIMKEEFSN DEEFHRRFRN
ESQAVAKLSH NNIVSIFDVS PSNSPVQYIV MELIEGITLK NYLQRKGSLS WQETLFFAQQ
ISKALSHAHS RGIIHQDIKP HNIILLRDGT VKVTDFGIAR FEKNQETRVI QEAIGSVHYI
SPEQAKGSRI DHRADLYSLG VVMYEMLTGR VPFDGDTPIA IVMQHINAQA PLPSELVPGI
PRGMDDIVMR AMCPVLSQRY ASADDIYNDL ERLKNNPNLR FTSAGAEARM PGGGRAATDE
TIALPRMNRQ QAAAATAHSR SFDDPQPQDQ VYRPSQKPSQ SRSTPADRDR RDRYEAEDED
GRRSSKRKKK KRSLSDSPAA MAGIAVAVFV MIAAGVAVFM MQAGNLFSSS GKVDVPNLVG
MQLQDAQSQY GNDFIIVEGE SRADENAEDG EILEQDPASG KVDKNSQITV VVCDNEEEDT
KDEDVIVLDE SIIGGILGED YQAVENKLTG LGLEVQIEHK NDQTVEKDKV ISISPELGRE
VKKGDTIYLY VSDGPEAVEL PNVVGKDISA ARAELNALNF TSINTSEEYN DAPAGQVFRQ
SPDSGEKIMP DTSITLYISK GPENNNNDSD NQENNNSDSN QSSDPEQSGN GDPEQSGSSG
GSTGTGDGSY EISIPINAQN TVTLSVELGD GTVLHSGPYD PSNGAFTYTV HGPVGQSETV
KYYINGNANS FTFMYR
//
