ID Q1G9I4_LACDA Unreviewed; 674 AA. AC Q1G9I4; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 100. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:CAI98210.1}; DE EC=2.7.1.- {ECO:0000313|EMBL:CAI98210.1}; GN OrderedLocusNames=Ldb1409 {ECO:0000313|EMBL:CAI98210.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM OS 00102 / Lb 14). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI98210.1, ECO:0000313|Proteomes:UP000001259}; RN [1] {ECO:0000313|EMBL:CAI98210.1, ECO:0000313|Proteomes:UP000001259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14 RC {ECO:0000313|Proteomes:UP000001259}; RX PubMed=16754859; DOI=10.1073/pnas.0603024103; RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P., RA Weissenbach J., Ehrlich S.D., Maguin E.; RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive RT and ongoing reductive evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006). 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 --------------------------------------------------------------------------- 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; CR954253; CAI98210.1; -; Genomic_DNA. DR AlphaFoldDB; Q1G9I4; -. DR STRING; 390333.Ldb1409; -. DR KEGG; ldb:Ldb1409; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR BioCyc; LDEL390333:LDB_RS06045-MONOMER; -. DR Proteomes; UP000001259; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. 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:CAI98210.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001259}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CAI98210.1}; KW Transferase {ECO:0000313|EMBL:CAI98210.1}; 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 18..278 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 357..424 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 425..492 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 507..573 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT BINDING 47 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 674 AA; 73680 MW; 5E7AF2C75BFF2380 CRC64; MRRMARVINK GYLLGDRYRI VDTLGEGGMA NVYLADDIIL KRQVAVKIIR LDLQKDSQVL ARFQREALAT SELSHPNIVS VFDVGTDHGL PYMVMEYVKG PDLKEYIREK SPIPLPQVIK IMDQILSAME LAHKHNVIHR DLKPQNILMD EKGNIKIADF GIAVALNQSA ITQTNSVLGS VHYMSPEQTR GGMVTKQSDI YSLGIILYEA LTGHVPFNGE TPVAIALKHA EDDIPSLRKQ NKAIPQALEN VVLKATAKDP RDRYASVAEM KADLDSSLDP SRAGEAIYRP SHGNNDETKI LPALNGKVMQ AEKAKEGKAE EPKKRSFWAS IKKYKWWWIG SLFPVFAILL FMFLAVGHNN VRVPDVVNMT EKAAKTSLKS SGLAVGAVKR TYSSDVKKGK VISTTPKANS PVDKGGKVNL LVSKGSNLTK VPDVEGLYLS TAKKKLNKLG FKVKSREAPS NEYLPGLIIS QSVKAGRKVD ASKTTITLVV AVALEDQPKP SSSSSSKKAT FKLADLTGKS LEDAQSYAKS KKLNVKVEKD HSDSVDSGDV IYTDPAAGSE VSEGDTLTIT VSKGAEKKEV KKTFTVDYQA AESSSNSSES SSSSSSSQGN HVRIYIQDDD HSLGNIYRDL YITKDTDFTI TFSVTKGDGK IKIVRDDQTV VDETISADDS ESGN //