ID B1HSW9_LYSSC Unreviewed; 794 AA. AC B1HSW9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 78. DE SubName: Full=Stage II sporulation protein E {ECO:0000313|EMBL:ACA37723.1}; DE EC=3.1.3.16 {ECO:0000313|EMBL:ACA37723.1}; GN OrderedLocusNames=Bsph_0085 {ECO:0000313|EMBL:ACA37723.1}; OS Lysinibacillus sphaericus (strain C3-41). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus. OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA37723.1, ECO:0000313|Proteomes:UP000002164}; RN [1] {ECO:0000313|EMBL:ACA37723.1, ECO:0000313|Proteomes:UP000002164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA37723.1, RC ECO:0000313|Proteomes:UP000002164}; RX PubMed=18296527; DOI=10.1128/JB.01652-07; RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., RA Berry C., Yuan Z.; RT "Complete genome sequence of the mosquitocidal bacterium Bacillus RT sphaericus C3-41 and comparison with those of closely related Bacillus RT species."; RL J. Bacteriol. 190:2892-2902(2008). 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; CP000817; ACA37723.1; -; Genomic_DNA. DR RefSeq; WP_012291893.1; NC_010382.1. DR AlphaFoldDB; B1HSW9; -. DR EnsemblBacteria; ACA37723; ACA37723; Bsph_0085. DR KEGG; lsp:Bsph_0085; -. DR HOGENOM; CLU_017349_0_0_9; -. DR Proteomes; UP000002164; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR045768; SpoIIE_N. DR PANTHER; PTHR43156:SF12; STAGE II SPORULATION PROTEIN E; 1. DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1. DR Pfam; PF07228; SpoIIE; 1. DR Pfam; PF19732; SpoIIE_N; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SUPFAM; SSF81606; PP2C-like; 1. PE 4: Predicted; KW Hydrolase {ECO:0000313|EMBL:ACA37723.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24..47 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 67..93 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 137..161 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 173..195 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 201..231 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 564..776 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|SMART:SM00331" SQ SEQUENCE 794 AA; 90449 MW; BF77236FC390CD16 CRC64; MTSIDWYNTA DVDDRKLGIK KKQIFIGSLF FLTSFFLAQS VVFEAAVPFS VPFWAIIRTK YREYAKFVLF GSLAGCFFLG FGQVVILALQ IIMYECIMRF RYWRLPQSIA VSLAVLLVQF MWQGAMYQGL PPVLVQFYVG CEAALALIMT LFMQVLFVNS YEWFTSHWTY EKLGSGLVVF AAMLTGMQAV VFSYFSLPIF LLQLFICFGA LVGSVPLATV IGAVLGTLIG VAKLSFTGML SVATLTGLCA GMGAKGGRFG VAIGSILPSV FFLFYDATLP LDSVYFTSIA IGSVLFLTIP RKYSDKVRDK LFPQREEVLI ARQNWLTEHV TYKLEHFQHF VQFMKELVFE RFMTAPVEEA KEVSPMNTCL SCFRYDHCWG AQNNGMDKLM TDWFHMKGVG KESAIHRVEE QMRYKCVKST KIFEELDTEL YRERINGQYF HGKKMIALQL RDMSNHLNQL IAEMKEDTVS FVSVEKDIIE RLKDAHIECF QLDVLNNKPG ARKIVCALAP ARVDWEKDTT LAERMILPIL YEIFNEPFEI EKVVACEIPF RHIQICFRSA ISFEVEYDIY SMSKDATLYS GDSHALFQLH PGLFAILLSD GMGQSKEAQH ESRKLIHLMR ECLNYNMNPE TAMHTLHYVM SLKQQDDMYA TLDFALVDLQ HGDLWSWKAG GMSTYILRGK EIIKVESNAA PVGFLSISAV EAEKRKLKAG DVILMHSDGL FSSVADWDEQ EETFLAYAQQ VASTNNTIQE KLTTIMQSFQ DYFEIEDDCT VLMLEVTHVV PTWAVFRPAQ YSVS //