ID Q5WFL0_SHOC1 Unreviewed; 706 AA. AC Q5WFL0; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=prkC {ECO:0000313|EMBL:BAD64850.1}; GN OrderedLocusNames=ABC2315 {ECO:0000313|EMBL:BAD64850.1}; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD64850.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|EMBL:BAD64850.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD64850.1, RC ECO:0000313|Proteomes:UP000001168}; RA Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.; RT "Molecular cloning and nucleotide sequence of the gene for an alkaline RT protease from the alkalophilic Bacillus sp. KSM-K16."; RL J. Ferment. Bioeng. 78:105-108(1994). RN [2] {ECO:0000313|EMBL:BAD64850.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD64850.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=7632397; DOI=10.1007/s002530050437; RA Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K., RA Kawai S., Ito S.; RT "Purification and properties of an alkaline protease from alkalophilic RT Bacillus sp. KSM-K16."; RL Appl. Microbiol. Biotechnol. 43:473-481(1995). RN [3] {ECO:0000313|EMBL:BAD64850.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD64850.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=9278275; DOI=10.1093/protein/10.6.627; RA Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.; RT "High-resolution crystal structure of M-protease: phylogeny aided analysis RT of the high-alkaline adaptation mechanism."; RL Protein Eng. 10:627-634(1997). RN [4] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM- RT K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAD64850.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD64850.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=17429572; DOI=10.1007/s00792-007-0074-1; RA Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K., RA Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.; RT "Intragenomic diversity of the V1 regions of 16S rRNA genes in high- RT alkaline protease-producing Bacillus clausii spp."; RL Extremophiles 11:597-603(2007). 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; AP006627; BAD64850.1; -; Genomic_DNA. DR RefSeq; WP_011247158.1; NC_006582.1. DR AlphaFoldDB; Q5WFL0; -. DR STRING; 66692.ABC2315; -. DR KEGG; bcl:ABC2315; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000001168; 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 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; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 2. 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:BAD64850.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001168}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAD64850.1}; KW Transferase {ECO:0000313|EMBL:BAD64850.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 349..371 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 10..270 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 377..442 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 443..510 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 309..341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 576..619 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 480..495 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 595..613 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 706 AA; 78268 MW; D157754F1EFB67AA CRC64; MIGERIGGRY VVLDSIGGGG MANVYLALDV ILDRHVAVKV LQPQFSEDEQ FINRFRREAQ AATSLANPNI VNIYDVGEED NVYYIVMEYV RGRTLKQVIQ EEGPLDIAVA LDYFKQILYG VGHAHAMQIV HRDIKPQNIL ISENGEAKVT DFGIARAMTS ATITHTNSVM GSVHYLSPEQ ARGGHVTYRS DIYSLGIVLY EMVTGQIPFS GDTAVSIAIK HLQNDIPSVR ELVPSVPISV ENVIRKATQK DPLQRYESAE EMVWACDAAL SADAEEDLAF VEDTVSDETT KELPIIGAYA DKNLEDTIAV PSKPSNHQEE AEDDNVPESE ANTTSDDGNG VKKKKRKKWL WLSAVALAVL IGATVLAFTF WNALFFVPEQ EVPDVVNMTE AEAVEEIEAR NLRVETEEIA DENYDEGRVA RQNPQAGRVI KEGQPVKLFI SASKDEVKID DYQGLTLSSA TRLLEQKGFS VETQPREDNS EPENTVLSQS PSPDTMAVPA ETTVVLTYSV PESIQLDDLT NQTEDDVRAY FNSEGLRGSF SREYDDDIAE GRVISQSPEP LSTLERGDNV SVVLSRGPEP LQEQPGSPPA EVPEQPTDEA EDPVEETPTQ GEDDEGDPTM VYRVTQTIVV SEEQQADGQS FDIRIVGKDA DSQGDERVLV EETITETTDF EIDLRVSPSY TGSYDVYIND EFNRQSQIYT YTEEEE //