ID Q899H6_CLOTE Unreviewed; 798 AA. AC Q899H6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 106. DE SubName: Full=Stage II sporulation protein E {ECO:0000313|EMBL:AAO34850.1}; DE EC=3.1.3.16 {ECO:0000313|EMBL:AAO34850.1}; GN OrderedLocusNames=CTC_00201 {ECO:0000313|EMBL:AAO34850.1}; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34850.1, ECO:0000313|Proteomes:UP000001412}; RN [1] {ECO:0000313|EMBL:AAO34850.1, ECO:0000313|Proteomes:UP000001412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412}; RX PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of tetanus RT disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). 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; AE015927; AAO34850.1; -; Genomic_DNA. DR AlphaFoldDB; Q899H6; -. DR STRING; 212717.CTC_00201; -. DR KEGG; ctc:CTC_00201; -. DR HOGENOM; CLU_017349_1_0_9; -. DR Proteomes; UP000001412; 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; IPR014221; SpoII_E. DR InterPro; IPR045768; SpoIIE_N. DR NCBIfam; TIGR02865; spore_II_E; 1. 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:AAO34850.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001412}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37..65 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 97..114 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 146..167 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 188..209 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 215..244 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 251..268 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 274..290 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 581..794 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|SMART:SM00331" SQ SEQUENCE 798 AA; 90250 MW; F824CCD93DA9F221 CRC64; MIKMQYGIDI LPYERIKRRD EEGKSSKNIL IKELIKLIVY FLASFLISRV VMVNLMAPFG IAFLISNMLE EENSIKLTSA LGTIVGYISI HSSVKDIWMY LILVPLIILN SYILRNKKEK SIIKSVFILV FLEVTIYNRF KLHISPLMSI TNSIFQTSCV FSLYYIINYS KICAKGFKTK HLFNSEEIIS MCITLSLIIS GVRGLNIFGL SIRNIIALSI IVMIGYIKGS SVGGACGVAM GVIIGISTND MTTFVGVFGI CGLISGIFKE SGKVISGLSY VVAFAILKLY SDIGIQFEFR EVLLGGSIFL LIPNKIYKKI ETDLDWEMKS ENIKDDYISK VKDIVQEKLT EFSQLLLYMG DTLENLAENH NLQMKKKSSS IVEKLADRVC SGCNMKHMCW KREGFYTYSA FSELINNFEN KKKVIPNEIE RKCIKRSVLV KNAEEIIKNY IIDEMWKKRI NEYRNFLAEQ ITNISYSVEE LTENINSQVH FNKYLENDIR RILNKNKIKY QDIFAYNDKL GKIIVKIHLS PCGGKQKCIK EILPFINKVT GKIMCISDDC CNIDSNNERC EITLEESPKY HVATHAGAVC KDGETYSGDS YTYGKLKDGK YITVISDGMG SGPEAGQESN AAVNLIEKFA KIGFDRINAI NMVNSLMTIN FSENEKFSTV DLSDINLYTG EVDFMKVGAV PSFIKSNGKV EVISSKTLPI GVLDKVDVDL VKKDIDNGDI IVMLSDGVLD YDDTEIGKVD WIVKYLEETN MNKPEDICKD IMEKAKLLRK GKVKDDMTVV VSKVYSLY //