ID R5MJK8_9FIRM Unreviewed; 728 AA.
AC R5MJK8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative serine/threonine-protein kinase PrkC {ECO:0000313|EMBL:CCY89889.1};
GN ORFNames=BN519_00149 {ECO:0000313|EMBL:CCY89889.1};
OS Eubacterium sp. CAG:180.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262882 {ECO:0000313|EMBL:CCY89889.1, ECO:0000313|Proteomes:UP000018411};
RN [1] {ECO:0000313|EMBL:CCY89889.1, ECO:0000313|Proteomes:UP000018411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:180 {ECO:0000313|Proteomes:UP000018411};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY89889.1}.
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DR EMBL; CAZC010000004; CCY89889.1; -; Genomic_DNA.
DR AlphaFoldDB; R5MJK8; -.
DR STRING; 1262882.BN519_00149; -.
DR Proteomes; UP000018411; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
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; IPR045269; Atg1-like.
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; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 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:CCY89889.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018411};
KW Transferase {ECO:0000313|EMBL:CCY89889.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 361..429
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 430..496
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 499..564
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 655..722
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 298..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Polar 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 728 AA; 79415 MW; C23AA9A469302615 CRC64;
MENYCGKRLD GRYEIREIIG VGGMAVVYKA YDVIDDRIVA IKILKEEFLA NDEFRRRFKN
ESKAIAVLSH PNIVKVYDVS FGDRLQYIVM EYIEGITLKE YIEQQKVINW KEAVHFVTQI
LKALQHAHDK GIVHRDVKPQ NIMLLQDGTI KVTDFGIARF CRGDTRTMTE NAIGSVHYIS
PEQARGEITD DKADIYSVGV VMYEMLTGQL PFQSDSAVSV AIMQLQQEAK RPREINPDIP
LGLEQITLRA MQKNPKDRYH SAAEMLVDLD AFRRNPSIKF DYDYFVDNEP TKFVDSKAVN
GTAARQPVPA ERRPAAPAVN GDDDKNDDEK PANKTVPILI GIIAGLVVIA AIVTGILLGR
NVKKVEVPNF VGKNYIDDIM SNAEYNSNFK FETESVYSTD AEPGSVIKQT PDAGTKLRKG
KTVKLQIAYN DDSVMIEGII GLSSDDAEQK LKKAGFTTKI ITSYQKNVTP GLVFDSYPTE
GSYAEKGSLV TLYVSTDKNS NSVKVPSVEG YSADVAKQLI EAAGLKAKVT ETDSDKPKGT
VINQNPVGDS EADSGSTVEI VISSGTPAST TASVTVNLPN LSGSSTGTVK IYLNSDLYAT
YTDVLLNGGT KTYEISGKGA NNKYTIFIND QNVQEGKIDF TQTPAKVSDV KNGSYDDKVA
LPNVVGKDVS EAKKTLETSG FTNVKVVDEN GNSASSGKVE SMTPSGGGKV SPSTEIKLVV
KSATPDNG
//
