ID   SP2E_PRIMG              Reviewed;         585 AA.
AC   P49600;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   13-SEP-2023, entry version 98.
DE   RecName: Full=Stage II sporulation protein E;
DE            EC=3.1.3.16;
DE   Flags: Fragment;
GN   Name=spoIIE;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35985 / VT1660;
RX   PubMed=8830262; DOI=10.1046/j.1365-2958.1996.433963.x;
RA   Barak I., Behari J., Olmedo G., Guzman P., Brown D.P., Castro E.,
RA   Walker D., Westpheling J., Youngman P.;
RT   "Structure and function of the Bacillus SpoIIE protein and its localization
RT   to sites of sporulation septum assembly.";
RL   Mol. Microbiol. 19:1047-1060(1996).
CC   -!- FUNCTION: Normally needed for pro-sigma E processing during sporulation
CC       but can be bypassed in vegetative cells. Activates SpoIIAA by
CC       dephosphorylation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Polar septum. {ECO:0000250}.
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; U26836; AAB58072.1; -; Genomic_DNA.
DR   PIR; S71018; S71018.
DR   PIR; S73325; S73325.
DR   AlphaFoldDB; P49600; -.
DR   SMR; P49600; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protein phosphatase; Sporulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..585
FT                   /note="Stage II sporulation protein E"
FT                   /id="PRO_0000057793"
FT   TRANSMEM        40..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          355..565
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   NON_TER         1
SQ   SEQUENCE   585 AA;  65690 MW;  90E9ACF1D3E21D01 CRC64;
     TVGVVTGLIL SFANVSSLYE MSLLAFSGLL GGLLKDGKKL GARLGLVVGS LLIGLYAQAD
     QGLTTNLYES LTAVVLFLLT PSFVLKNLSK LVPGTSENML EQQQYVRKIR DVTANRVEQF
     SNVFQALSKS FTQNGFYDEK PSADKEVDYF LSSVTERTCQ FCFKKEQCWA QQFDTTYEYM
     KEIMLEVDNG TLEQNPRLIR EMDKHCVKSK KVIDVIEHEL TYFKANQHLK AQIQESRRIV
     AEQLHGVSEV MGNFAKEIKR ERENLNVQEE QILEALRNFG MEINQIEIYS LEPGNVDIEM
     WVPYCHGRGE CEKIIAPMLT DILGESIVVK NEECAKYPQG YCHVSFGCTK AYVVDTGVAH
     AAKGGGFVSG DSYSMIELNA GKYALAISDG MGNGERAHYE SSETLQLLKQ ILQTGIEETI
     AIKSINSILS LRTNDEIFST LDLAMIDLQD ANVNFLKIGS TPSFIKRGDK VIKIQASNLP
     MGIIEEFEVD VVNEQMKAED LLIMMSDGVF EGPKHVENYE MWMKRKIGEL QTNDPQEIAD
     LIMEEVIRTK VGLIEDDMTV VVAKLQHNTP KWSSIPSYAY RNLAQ
//