SP2E_PRIMG
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 03-AUG-2022, entry version 94.
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; Firmicutes; 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}.
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DR EMBL; U26836; AAB58072.1; -; Genomic_DNA.
DR PIR; S71018; S71018.
DR PIR; S73325; S73325.
DR AlphaFoldDB; P49600; -.
DR SMR; P49600; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR014221; SpoII_E.
DR InterPro; IPR045768; SpoIIE_N.
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; SSF81606; 1.
DR TIGRFAMs; TIGR02865; spore_II_E; 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