(data stored in SCRATCH zone)

SWISSPROT: SP3AE_BACSU

ID   SP3AE_BACSU             Reviewed;         399 AA.
AC   P49782;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Stage III sporulation protein AE;
DE   Flags: Precursor;
GN   Name=spoIIIAE; OrderedLocusNames=BSU24390;
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 / JH642;
RA   Guerout-Fleury A.M., Gonzy-Treboul G., Stragier P.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(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   SEQUENCE REVISION TO 29 AND C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION IN SPORULATION, INTERACTION WITH SPOIIIJ AND YQJG, SUBCELLULAR
RP   LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--ALA-24;
RP   3-ARG--GLN-23 AND ALA-24.
RC   STRAIN=168 / MB24;
RX   PubMed=18820020; DOI=10.1128/jb.00715-08;
RA   Serrano M., Vieira F., Moran C.P. Jr., Henriques A.O.;
RT   "Processing of a membrane protein required for cell-to-cell signaling
RT   during endospore formation in Bacillus subtilis.";
RL   J. Bacteriol. 190:7786-7796(2008).
CC   -!- FUNCTION: Required during sporulation for activation of sigma factor
CC       SpoIIIG/SigG after engulfment is completed in the prespore.
CC       Overexpression in the absence of SpoIIIJ is synthetically lethal.
CC       {ECO:0000269|PubMed:18820020}.
CC   -!- SUBUNIT: Interacts with SpoIIIJ and YqjG.
CC       {ECO:0000269|PubMed:18820020}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18820020};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:18820020}. Note=Signal
CC       sequence cleavage facilitates function; replacing the signal with the
CC       first transmembrane region of SpoIVFB decreases sporulation 7-fold,
CC       whereas replacing it with the SleB signal sequence does not affect
CC       sporulation.
CC   -!- DISRUPTION PHENOTYPE: 4000-fold reduction in sporulation efficiency.
CC       {ECO:0000269|PubMed:18820020}.
DR   EMBL; U35252; AAA76724.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12564.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14370.2; -; Genomic_DNA.
DR   PIR; H69711; H69711.
DR   RefSeq; NP_390319.2; NC_000964.3.
DR   RefSeq; WP_003230230.1; NZ_JNCM01000036.1.
DR   IntAct; P49782; 2.
DR   STRING; 224308.BSU24390; -.
DR   TCDB; 9.B.70.1.1; the multicomponent putative spoiiiae exporter (spoiiia-e) family.
DR   PaxDb; P49782; -.
DR   PRIDE; P49782; -.
DR   EnsemblBacteria; CAB14370; CAB14370; BSU24390.
DR   GeneID; 938569; -.
DR   KEGG; bsu:BSU24390; -.
DR   PATRIC; fig|224308.179.peg.2657; -.
DR   HOGENOM; HOG000057582; -.
DR   KO; K06394; -.
DR   OMA; EYGGFLP; -.
DR   PhylomeDB; P49782; -.
DR   BioCyc; BSUB:BSU24390-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR014194; Spore_III_AE.
DR   Pfam; PF09546; Spore_III_AE; 1.
DR   TIGRFAMs; TIGR02829; spore_III_AE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P49782.
DR   SWISS-2DPAGE; P49782.
KW   Cell membrane; Membrane; Reference proteome; Signal; Sporulation;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000305"
FT   CHAIN           25..399
FT                   /note="Stage III sporulation protein AE"
FT                   /id="PRO_0000072069"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         1..24
FT                   /note="MKRFQWVLLLAVLIIAGRAEIVQA->MNKWLDLILKIHVHPFLWIIAALGLL
FT                   TGHMK: 7-fold reduction in sporulation efficiency (first
FT                   SpoIVFB transmembrane region)."
FT                   /evidence="ECO:0000269|PubMed:18820020"
FT   MUTAGEN         1..24
FT                   /note="Missing: 200-fold reduction in sporulation
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:18820020"
FT   MUTAGEN         3..23
FT                   /note="RFQWVLLLAVLIIAGRAEIVQ->SKGSIMACLILFSFTITTFINTETIS:
FT                   No change in sporulation efficiency (SleB signal
FT                   sequence)."
FT                   /evidence="ECO:0000269|PubMed:18820020"
FT   MUTAGEN         24
FT                   /note="A->K: 10-fold reduction in sporulation efficiency.
FT                   Sigma factor G (SigG) is not activated, signal sequence is
FT                   not cleaved."
FT                   /evidence="ECO:0000269|PubMed:18820020"
FT   CONFLICT        29
FT                   /note="E -> G (in Ref. 2; BAA12564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        367..398
FT                   /note="VIYIFAALAIVSLMFFLSLTVIITAGNLTMMM -> GHLYFCSSRHCVSHVF
FT                   FKPYCHNHSRKPHDDDEMKEAG (in Ref. 2; BAA12564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  42921 MW;  57EB1849364E9A9A CRC64;
     MKRFQWVLLL AVLIIAGRAE IVQAAGNAEQ TEDHAETAEQ LAERTAASLE TDKIGEFWND
     IMTEYGGLLP ESQKGSLMEF INGDKSFSPQ EWLKALFSYL FHEVLANGKL LGTLILLTIF
     CVILQLLQNA FQQSTVSKVA YSIVYMVLII LALNSFHVAI NYATEAIQTM TSFILALIPL
     LLALLASSGG AVSAAFFHPV ILFLMNTSGL LIQNIVMPLI FLSAILSIVS TMTEQYKVTQ
     LANLLRNIAI GALAVFLTIF LGVISVQGAS AAVTDGITLR TAKFITGNFI PVLGRMFTDA
     TDTVISASLL LKNTVGILGV AILICIAAFP AIKVLSLAFI YKLAAAILQP LGGGPVITCL
     DVISKSVIYI FAALAIVSLM FFLSLTVIIT AGNLTMMMK
//

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