ID Q92AI8_LISIN Unreviewed; 657 AA. AC Q92AI8; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=lin1934 {ECO:0000313|EMBL:CAC97164.1}; OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=272626 {ECO:0000313|EMBL:CAC97164.1, ECO:0000313|Proteomes:UP000002513}; RN [1] {ECO:0000313|EMBL:CAC97164.1, ECO:0000313|Proteomes:UP000002513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000313|Proteomes:UP000002513}; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D., RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M., RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E., RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C., RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). 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; AL596170; CAC97164.1; -; Genomic_DNA. DR PIR; AD1674; AD1674. DR RefSeq; WP_003769293.1; NC_003212.1. DR AlphaFoldDB; Q92AI8; -. DR STRING; 272626.gene:17566292; -. DR KEGG; lin:lin1934; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000002513; 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-EC. 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 Pfam; PF21160; PrkC-like_PASTA-like; 1. DR SMART; SM00740; PASTA; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 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}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 341..362 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 11..271 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 365..432 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 433..501 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 502..568 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 657 AA; 72245 MW; F00DD440A9A8E0F0 CRC64; MMIGKRLNDR YKILHAIGGG GMANVYLAHD IILDRDVAVK ILRIDLADES NLIRRFQREA QSATSLVHPN IVSVYDVGEE NDLHYIVMEH VDGMDLKQYI QENHPISYDK AVDIMLQIVS AVAIAHQHHI IHRDLKPQNI LIDHDGVVKI TDFGIAMALS ETSITQTNSL LGSVHYLSPE QARGGMATQK SDIYSLGIVL YELLTGKVPF DGESAVSIAI KHLQAEIPSA RAQNPEIPQS LENIIIKATA KDPFLRYQNA EEMEKDLQTC LNKDRLNEPK YVFPTNDDDG DTKTIPIIAT KEAMQNLDKT IVPEGKVAAE EVAVDDKKGK KKKKMSKKKK IILIVSSVIV LFIIGILLLW LLGKSPDEVA VPDVSGKTED QAIALLQKDG FVIGKTAEKN SDDVEEGKVI NTDPSAGEMK EKGTKINLFV SIGSKKITME DYTGRSYSET KTLLEQQGFN NISAEEAYSS EVGKGMIISQ TPTQGTEVVA KSTDVKFVVS KGAEPITLKD LRGYTKTAVE DYASPLGLKV SSKEENSNSV EKGQVISQSP SAGTAINAGD TIEIVISAGP KEKQVKEVTK TFNIPYTPSD EENPQPQKVQ IYIQDKDHSM TSAYREMNIT QNTSVEVTFQ IEEGSSAGYK IISDDKVIDE GTVPYPN //