ID A0A0K2LCV2_9LACO Unreviewed; 654 AA.
AC A0A0K2LCV2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=JP39_06960 {ECO:0000313|EMBL:ALB29126.1};
OS Companilactobacillus heilongjiangensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1074467 {ECO:0000313|EMBL:ALB29126.1, ECO:0000313|Proteomes:UP000061546};
RN [1] {ECO:0000313|EMBL:ALB29126.1, ECO:0000313|Proteomes:UP000061546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28069 {ECO:0000313|EMBL:ALB29126.1,
RC ECO:0000313|Proteomes:UP000061546};
RA Jiang X., Zheng B., Cheng H.;
RT "Genomic sequence of Lactobacillus heilongjiangensis DSM 28069, isolated
RT from Chinese traditional pickle.";
RL Submitted (AUG-2015) 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};
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DR EMBL; CP012559; ALB29126.1; -; Genomic_DNA.
DR RefSeq; WP_041499621.1; NZ_CP012559.1.
DR AlphaFoldDB; A0A0K2LCV2; -.
DR STRING; 1074467.JP39_06960; -.
DR KEGG; lhi:JP39_06960; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000061546; Chromosome.
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-KW.
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:ALB29126.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ALB29126.1};
KW Transferase {ECO:0000313|EMBL:ALB29126.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 323..343
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 345..412
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 413..480
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 485..551
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 548..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Polar 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 654 AA; 71682 MW; 05A7C0EA66E5F419 CRC64;
MEKGYLVGGR YEILGTLGEG GMANVYLAND TLLNRKVAVK ALRYDLQDDE SVKRRFGREA
KATSGLSNPN IVNVLDVGND DGVQYIVIEY VDGPNLKKYI RTHFPIPYRE VVDIMKQICM
AVSDAHEHGI IHRDLKPENI LVDEKKDPIQ VKVSDFGIAL ALSERSITRT NSLLGSVHYM
SPEQIKGRSA TVLSDIYALG IILFELLTKH VPFTGDTAVT VALKHSKEEM PDLKKIDPNI
PQPLENAVLK ATAKDPDQRY QSVREMCDDL NTCLMPERAD EPKFIPTPIN NLEETRVMEP
LDAAVEKSAP EKKPQKMSRR RKLILLASMV PLVLILFIVA MVIKSNQETT VPDLYNLTVK
QANVILKSSN LSVGDVSKEN DDDVDAGHVI KSIPAKGLKL KNGAKVNLVV SLGATYYKMP
KLVGKQYEDV SDNLKRRGFK VKVDYKATNQ YDAGTIIKQS IPRGKKVVTK NKSLTLTVAK
IKTVKPKVVK VRDLTGYNLK SIQDYASETG LTLNTSYEYS DEIESGLLIS QTPTANSTIS
QGGTLSVVMS KGADPDKSSS DKDDSDSEHN GSSSNSSGTS TVTKDITIPY DSSGSNNVTI
YISDATHSIG TVYKTMTITG DTPVTLSFNL KDGQTGSYIV ERNNKTVLGG SVNG
//
