ID C6LBW8_9FIRM Unreviewed; 643 AA.
AC C6LBW8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Leucine Rich Repeat protein {ECO:0000313|EMBL:EET61921.1};
GN ORFNames=BRYFOR_06113 {ECO:0000313|EMBL:EET61921.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET61921.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET61921.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET61921.1,
RC ECO:0000313|Proteomes:UP000005561};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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:EET61921.1}.
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; ACCL02000004; EET61921.1; -; Genomic_DNA.
DR RefSeq; WP_006860910.1; NZ_CP102268.1.
DR AlphaFoldDB; C6LBW8; -.
DR STRING; 168384.SAMN05660368_00536; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG4886; Bacteria.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000005561; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46652; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46652:SF3; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 9 ISOFORM X1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 643 AA; 73128 MW; 56DAAD584A469477 CRC64;
MNREKQTRVP RQEESLQKWY IQEQELPEAL KKEFHIVSCL SWQEEQSVYL LEDKAGRRSV
IKRAEEKRKE VLRKEAECLK RIPFSFLPAF LSWQEEDGAG WLQREYIPGD TLWELVERNG
PLEAEKAGEI LCRLCGIAGQ LHRCDPPIIH RDFKPQNIVL TPEGNLFLID LGTVRAYREG
AAHDTQFMGT RQTAAPEQYG YRQTDCRTDI YALGVIYLYL LTGSMELQRP ENLSGVPEGC
RRIIEKCTRM EPEERYASAE ELERAVRETT GGAAEGDAKH AQRRKRKWLL PVLFVAALAL
LGISGICYYR EMPYQFHSEL VEEAVRRQLG RTDGQAITKE ELAGIESLRI CGDYILTENE
QHQQHSASHS VDGTEISGSG NISDLTDLVY MKNLRTLVLD RQEITDISPL AALPLESVSL
CRNPVTDISA LSGMDTLREL YLEETGVQSL EDMAEMTSLR VLRIGNEQPV DLTPVAELPL
EELCMVMVAE DSTEILQKLP LKRLRFHSWS MELEEAVGQM TDLEELTIYG YQYDTLLSLL
SLTDLRTLDL YGGRLQSVEG IEALAKLTFL GINNTPVQDI SPLAALEQLT WLGLDNTEIT
DFSVLTELKN LQWVRCDEVQ RPQIEDMADT LPFTLESVPV TEE
//