ID A0A0R1JB12_9LACO Unreviewed; 648 AA.
AC A0A0R1JB12;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=FC72_GL000093 {ECO:0000313|EMBL:KRK65649.1};
OS Companilactobacillus tucceti DSM 20183.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1423811 {ECO:0000313|EMBL:KRK65649.1, ECO:0000313|Proteomes:UP000050929};
RN [1] {ECO:0000313|EMBL:KRK65649.1, ECO:0000313|Proteomes:UP000050929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20183 {ECO:0000313|EMBL:KRK65649.1,
RC ECO:0000313|Proteomes:UP000050929};
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:KRK65649.1}.
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DR EMBL; AZDG01000001; KRK65649.1; -; Genomic_DNA.
DR RefSeq; WP_057763651.1; NZ_AZDG01000001.1.
DR AlphaFoldDB; A0A0R1JB12; -.
DR STRING; 1423811.FC72_GL000093; -.
DR PATRIC; fig|1423811.3.peg.92; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000050929; 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; 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; 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; 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:KRK65649.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000050929};
KW Transferase {ECO:0000313|EMBL:KRK65649.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 320..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 341..408
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 409..476
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 481..547
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 546..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 648 AA; 71229 MW; 0F315D742D970BB2 CRC64;
MDKGYLVGGR YEILGTLGEG GMANVYLAKD IRLNRKVAVK ALRYDLQDDE SVKRRFGREA
KATSGLSSPN IVNVLDVGND NGIQFIVIEY VDGPNLKRYL KTHFPIPYHE VVDIMEQICS
AVTTAHEHGI IHRDLKPENI LVDDSKDPIQ VKVSDFGIAL ALSDQSITRT NSLLGSVHYM
SPEQIRGKSA TVLSDIYALG IILFELLTKH VPFTGDTAVS VALKHSKEDI PDLHAIDHNI
PQPLENVVLR ATAKDPEERY QTVREMCEDI DTCLLPERAS EPKFVPISHN DLEETKVMQP
LREDDQDKSA NKKKSKRNKI IWMSLIPLLL LLFLIFAIVR GSAETSVPDL SNLTIKQATV
MLKGSNLQVG SISKENDDDV IAGHVIKSIP AKGLKLKNNA KVNLVVSLGA RYYKMPKVTG
KQYDEVSDGL KKRGFTIHLK YKETNEYSAG VVMKQSIKAG SKVVAKKKRL VLTIAKTPTV
KKKTYKVRDL TGYNLKSIQD YADEIDAVLD VTYQYSDTVT SGMLISQNPS AGSSISQGAT
LTVVMSKGKE ESDSNSSDSD KDNDNNNDSG TKTVTKEVSI PYDDGGGTSN SVTIYIGDAN
HNISNPYKTM TITQTTPVTL SFNLKSGQTG TYNIVRDNQT VVTGSVSG
//
