ID A0A0R1U8K3_9LACO Unreviewed; 670 AA.
AC A0A0R1U8K3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Non-specific serine threonine protein kinase {ECO:0000313|EMBL:KRL89661.1};
GN ORFNames=FC46_GL000564 {ECO:0000313|EMBL:KRL89661.1};
OS Lactobacillus kalixensis DSM 16043.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423763 {ECO:0000313|EMBL:KRL89661.1, ECO:0000313|Proteomes:UP000051036};
RN [1] {ECO:0000313|EMBL:KRL89661.1, ECO:0000313|Proteomes:UP000051036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16043 {ECO:0000313|EMBL:KRL89661.1,
RC ECO:0000313|Proteomes:UP000051036};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL89661.1}.
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DR EMBL; AZFM01000019; KRL89661.1; -; Genomic_DNA.
DR RefSeq; WP_057798945.1; NZ_AZFM01000019.1.
DR AlphaFoldDB; A0A0R1U8K3; -.
DR STRING; 1423763.FC46_GL000564; -.
DR PATRIC; fig|1423763.3.peg.568; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000051036; 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; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.40.2560; -; 1.
DR Gene3D; 3.30.10.20; -; 3.
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; 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; 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:KRL89661.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:KRL89661.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 361..428
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 429..496
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 503..569
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 585..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..616
FT /note="Basic and acidic 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 670 AA; 74341 MW; 8E79B1B92EADE961 CRC64;
MIDKGYLLGE RYRIIDTLGE GGMANVYLAE DIILQRKVAV KVLRLDLKKD PQTEARFQRE
ALATSELSHP NIVSVLDVGN DQGLPYMVME YVDGPDLKDY IRMNSPLSLH EIIHIMDQIL
SAVALAHKHN VIHRDLKPQN ILMDKRGNVK IADFGIAVAL NQSSVTQTNS IMGSVHYMSP
EQTRGGLVTK QSDIYSLGII LYELITGHVP FNGDTPVAVA LKHAQEPIPS IRKNSPSVPQ
ALENVVLKAT AKDPRDRYAS AQEMKADLDT SLDFSRKDEP IFVPSHGANN DETIILPGFK
PQIKEESSTV QEEKTNPKDE KTSKAGFWQN FKKHKWWYIF IGITAFLIVF IMIFALNGRS
NNEQIHVPDV TNVAEGSAKQ RIEEAGLVVG TVTRKHSDSI DAGKVIETKP SAGDALNRGS
RVDIVVSSGA GMTKVPDVVN EEYEDALKKL QDLGFDVIRE NQYSSRVPKN QIISQSIAAG
VQVKPKQTTI TLVVSQGRAP KPKSNMIKLR DLAGSTLEAA QDYAREHGLT LQINQEYSDT
VKKDRIISMQ PEAGTSVEKG STITVSVSKG EKEQTEETNV TKTFTVNYED NADSSDDDGA
TDQTTQDKEE KGNHVQIYIK DDDHSLGNIY RDLYIKRDMS FSIPFSLKDG DGQLRVVRDG
KTILNEKVTK
//
