SP2E_BACSU
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 03-AUG-2022, entry version 153.
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; Firmicutes; 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; P37475; -.
DR PRIDE; P37475; -.
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 OMA; HNTPKWA; -.
DR PhylomeDB; P37475; -.
DR BioCyc; BSUB:BSU00640-MON; -.
DR BRENDA; 3.1.3.16; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0042601; C:endospore-forming forespore; IDA:CACAO.
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:0016791; F:phosphatase activity; IBA:GO_Central.
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 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
