ID Q4L5S1_STAHJ Unreviewed; 675 AA. AC Q4L5S1; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 135. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE05004.1}; GN OrderedLocusNames=SH1695 {ECO:0000313|EMBL:BAE05004.1}; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE05004.1, ECO:0000313|Proteomes:UP000000543}; RN [1] {ECO:0000313|EMBL:BAE05004.1, ECO:0000313|Proteomes:UP000000543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE05004.1, RC ECO:0000313|Proteomes:UP000000543}; RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., RA Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). 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; AP006716; BAE05004.1; -; Genomic_DNA. DR RefSeq; WP_011275980.1; NC_007168.1. DR AlphaFoldDB; Q4L5S1; -. DR GeneID; 58062115; -. DR KEGG; sha:SH1695; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000000543; 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 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:SF74; KINASE, PUTATIVE-RELATED; 1. DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 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; 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 345..367 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 368..435 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 436..504 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 505..570 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 534..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 534..571 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 572..601 FT /note="Basic and 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 675 AA; 76082 MW; 3257EE48CAAE3A09 CRC64; MIGKIVSERY KIVDKLGGGG MSTVYLAEDT ILNREVAIKA ISIPQNEKEE TMKRFEREVN NATQLSHENI VEVYDVQEDE ECFFLIMEYI DGPTLSEYIH SHGPLSVDTA IDFTNQILKG VAQAHEKLII HRDIKPQNIL IDKNKTLKIF DFGIAKALSE TSMTQTNHVL GTVQYLSPEQ AKGETTNEAT DIYSIGIVLY EMLVGEPPFN GETAVSIAIK HIQDSIPNVT ELRSEIPQSL SNVVLRATEK KASDRYQSVK DMKEDLSSVL VSSRANEKKH SIEEDETNTV SIDRQDIKSK IKEENEQKQI AQTMQIPIVN EHHFQTSEAQ IYEPPKKKRS KKKKFAIALI LLLLVASLFG FIAMGMFGSK YAEVPDLKGK TEKEAEKILR QSHLEIGNIS RDYSDDYPEN KIIKTKPKQG ERVNQHEKVD IVLSKGPERA KMPNVIGMKK VDALDKLKQS KLDHVTVNQE YNNQVPKGAI AKQSVNPDSY VRINDHQITL TESLGVKKVY VKNYENKNYQ TAKKELEKNG LKVQMTTESS NNVKKDNIIS QSPKNTEVEE GSTVQFIVSK GKTSSKDEDK DSEKSKSSSE DKSDDTQKVK NYTETYHIPY TGDDESQKVQ VYIRDKDNSG TSASQTFSIK DDKTITIPLK IEQGSDAGYT IRVDGDVIAD KDIEY //