ID   SP2E_BACSU              Reviewed;         827 AA.
AC   P37475;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Stage II sporulation protein E;
DE            EC=3.1.3.16;
DE   AltName: Full=Stage II sporulation protein H;
GN   Name=spoIIE; Synonyms=spoIIH; OrderedLocusNames=BSU00640;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX   PubMed=2832371; DOI=10.1128/jb.170.4.1598-1609.1988;
RA   Guzman P., Westpheling J., Youngman P.;
RT   "Characterization of the promoter region of the Bacillus subtilis spoIIE
RT   operon.";
RL   J. Bacteriol. 170:1598-1609(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC   STRAIN=168;
RX   PubMed=8113187; DOI=10.1128/jb.176.5.1451-1459.1994;
RA   Levin P.A., Losick R.;
RT   "Characterization of a cell division gene from Bacillus subtilis that is
RT   required for vegetative and sporulation septum formation.";
RL   J. Bacteriol. 176:1451-1459(1994).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=7570023; DOI=10.1126/science.270.5236.641;
RA   Duncan L., Alper S., Arigoni F., Losick R., Stragier P.;
RT   "Activation of cell-specific transcription by a serine phosphatase at the
RT   site of asymmetric division.";
RL   Science 270:641-644(1995).
CC   -!- FUNCTION: Normally needed for pro-sigma E processing during sporulation
CC       but can be bypassed in vegetative cells. Activates SpoIIAA by
CC       dephosphorylation.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- INTERACTION:
CC       P37475; P45870: racA; NbExp=3; IntAct=EBI-9304781, EBI-5242400;
CC       P37475; P16971: recA; NbExp=2; IntAct=EBI-9304781, EBI-1535844;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Polar septum.
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DR   EMBL; D26185; BAA05299.1; -; Genomic_DNA.
DR   EMBL; U26835; AAB58073.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11840.1; -; Genomic_DNA.
DR   EMBL; M29403; AAA22798.1; -; Genomic_DNA.
DR   EMBL; L23497; AAB38381.1; -; Genomic_DNA.
DR   PIR; S66094; S66094.
DR   RefSeq; NP_387945.1; NC_000964.3.
DR   RefSeq; WP_003243026.1; NZ_JNCM01000028.1.
DR   PDB; 3T91; X-ray; 2.64 A; A/B=590-827.
DR   PDB; 3T9Q; X-ray; 2.76 A; A/B=590-827.
DR   PDB; 5MQH; X-ray; 2.45 A; A=590-827.
DR   PDB; 5UCG; X-ray; 3.91 A; A/B/C/D/E=465-809.
DR   PDBsum; 3T91; -.
DR   PDBsum; 3T9Q; -.
DR   PDBsum; 5MQH; -.
DR   PDBsum; 5UCG; -.
DR   AlphaFoldDB; P37475; -.
DR   SMR; P37475; -.
DR   IntAct; P37475; 16.
DR   STRING; 224308.BSU00640; -.
DR   PaxDb; 224308-BSU00640; -.
DR   DNASU; 938480; -.
DR   EnsemblBacteria; CAB11840; CAB11840; BSU_00640.
DR   GeneID; 938480; -.
DR   KEGG; bsu:BSU00640; -.
DR   PATRIC; fig|224308.179.peg.64; -.
DR   eggNOG; COG2208; Bacteria.
DR   InParanoid; P37475; -.
DR   OrthoDB; 9763774at2; -.
DR   PhylomeDB; P37475; -.
DR   BioCyc; BSUB:BSU00640-MONOMER; -.
DR   BRENDA; 3.1.3.16; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0042601; C:endospore-forming forespore; IDA:CACAO.
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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Hydrolase; Membrane; Protein phosphatase;
KW   Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..827
FT                   /note="Stage II sporulation protein E"
FT                   /id="PRO_0000057794"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..827
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          594..804
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   STRAND          590..600
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   HELIX           602..604
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          609..615
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   TURN            618..620
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          621..628
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   HELIX           634..651
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   TURN            652..654
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   HELIX           657..669
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          673..675
FT                   /evidence="ECO:0007829|PDB:3T91"
FT   STRAND          679..686
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   TURN            687..689
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          691..699
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          702..706
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          709..713
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          728..734
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          740..744
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   HELIX           746..749
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          752..754
FT                   /evidence="ECO:0007829|PDB:3T9Q"
FT   HELIX           758..767
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   HELIX           774..788
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   TURN            789..791
FT                   /evidence="ECO:0007829|PDB:5MQH"
FT   STRAND          797..806
FT                   /evidence="ECO:0007829|PDB:5MQH"
SQ   SEQUENCE   827 AA;  91969 MW;  33EA3A81935B407B CRC64;
     MEKAERRVNG PMAGQALEKL QSFFNRGTKL VTHHLHSLFF YKGFIYVVIG FLLGRAFILS
     EVLPFALPFF GAMLLIRRDK AFYAVLAVLA GALTISPKHS LLILAALLAF FVFSKVAAFI
     TDDRVKALPI VVFFSMAAAR AGFVYAQNGV FTTYDYVMAI VEAGLSFILT LIFLQSLPIF
     TVKKVKQSLK IEEIICFMIL IASVLTGLAG LSYQGMQAEH ILARYVVLSF SFIGGASIGC
     TVGVVTGLIL GLANIGNLYQ MSLLAFSGLL GGLLKEGKKA GAAIGLIVGS LLISLYGEGS
     AGLMTTLYES LIAVCLFLLT PQSITRKVAR YIPGTVEHLQ EQQQYARKIR DVTAQKVDQF
     SNVFHALSES FATFYQASDE QTDDSEVDLF LSKITEHSCQ TCYKKNRCWV QNFDKTYDLM
     KQVMLETEEK EYASNRRLKK EFQQYCSKSK QVEELIEDEL AHHHAHLTLK KKVQDSRRLV
     AEQLLGVSEV MADFSREIKR EREQHFLQEE QIIEALQHFG IEIQHVEIYS LEQGNIDIEM
     TIPFSGHGES EKIIAPMLSD ILEEQILVKA EQHSPHPNGY SHVAFGSTKS YRVSTGAAHA
     AKGGGLVSGD SYSMMELGAR KYAAAISDGM GNGARAHFES NETIKLLEKI LESGIDEKIA
     IKTINSILSL RTTDEIYSTL DLSIIDLQDA SCKFLKVGST PSFIKRGDQV MKVQASNLPI
     GIINEFDVEV VSEQLKAGDL LIMMSDGIFE GPKHVENHDL WMKRKMKGLK TNDPQEIADL
     LMEEVIRTRS GQIEDDMTVV VVRIDHNTPK WASIPVPAIF QNKQEIS
//