ID L1QF53_9CLOT Unreviewed; 689 AA.
AC L1QF53;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative serine/threonine-protein kinase PrkC {ECO:0000313|EMBL:EKY26629.1};
GN ORFNames=HMPREF0216_01814 {ECO:0000313|EMBL:EKY26629.1};
OS Clostridium celatum DSM 1785.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY26629.1, ECO:0000313|Proteomes:UP000010420};
RN [1] {ECO:0000313|EMBL:EKY26629.1, ECO:0000313|Proteomes:UP000010420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY26629.1,
RC ECO:0000313|Proteomes:UP000010420};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-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:EKY26629.1}.
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DR EMBL; AMEZ01000053; EKY26629.1; -; Genomic_DNA.
DR RefSeq; WP_005213504.1; NZ_KB291645.1.
DR AlphaFoldDB; L1QF53; -.
DR STRING; 545697.HMPREF0216_01814; -.
DR GeneID; 85156546; -.
DR PATRIC; fig|545697.3.peg.1784; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000010420; 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 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; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
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:EKY26629.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000010420};
KW Transferase {ECO:0000313|EMBL:EKY26629.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..438
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 439..505
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 506..575
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 313..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 689 AA; 75337 MW; 870AEF0DE032E395 CRC64;
MIGEVLGERY ELLEKIGEGG MAIVYKARDR KLDRLVAVKI LKKEFANNKD VAEKFKKEAT
AVANFSNSNI VNVLDVGHEE DGNVDYFVME YINGKTLKEF IKYNGKLTYT TAINIAIKIA
KALECAHGNN IIHRDVKPQN ILVTESGEVK VTDFGIAKSS TSSTITNTTT IMGSAHYLSP
EQAKGSFIDF RSDIYSLGIV LYEMVTGKLP FDGESPVTVA LKHIQEEPIE PKAINASIPN
SLNALIMKCI NKEPINRYES CRELIKDLQT IKDNPDVNLN TAIDDGRTII MEPIKVDNKQ
NISKPNIYTK ADFEKDYSGE SEEESDDKNE KNRQIPSNKK ISKKLIIGIV ITLLLLVGGI
VGAVVLGSNN ATTAEIPVPN IIGMDVEVAK KKLEELGLKL EIVGTSESDR PENSVLESIP
EASAMVDKGS TVKVTISGGE EKVKVPDLRD YEVNYIKEVL TRLGLKYEIT EEYSDVVEQG
YLISQNPEKN TEVVKDTVIK LTISSGPEVK IVLIENYLGE NIEEAQRKLE DLGLVVQVVE
QETDRESENG IVIQQSLQRG NKVGVGTPIT LTYGKYVDPT VDVSQYIYIG MNLSDAIAVL
DGANISYTIS GGSPSQESMN TYTIKGFTEN IKKGELVKLQ IEKIPQTPSG DNNSNNGNDA
ESGNNGNSGN GGNSADNGGD NNSAEVPNP
//
