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 03-AUG-2022, entry version 110.
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}.
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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 AlphaFoldDB; P49782; -.
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; BSU_24390.
DR GeneID; 938569; -.
DR KEGG; bsu:BSU24390; -.
DR PATRIC; fig|224308.179.peg.2657; -.
DR eggNOG; ENOG502Z7PW; Bacteria.
DR OMA; EYGGFLP; -.
DR PhylomeDB; P49782; -.
DR BioCyc; BSUB:BSU24390-MON; -.
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;
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
