ID   SP4FA_BACSU             Reviewed;         264 AA.
AC   P26936;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Stage IV sporulation protein FA;
GN   Name=spoIVFA; Synonyms=bofB; OrderedLocusNames=BSU27980;
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=1942049; DOI=10.1016/0022-2836(91)90931-u;
RA   Cutting S.M., Roels S., Losick R.;
RT   "Sporulation operon spoIVF and the characterization of mutations that
RT   uncouple mother-cell from forespore gene expression in Bacillus subtilis.";
RL   J. Mol. Biol. 221:1237-1256(1991).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC   STRAIN=168;
RX   PubMed=8459776; DOI=10.1111/j.1365-2958.1993.tb01151.x;
RA   Lee S., Price C.W.;
RT   "The minCD locus of Bacillus subtilis lacks the minE determinant that
RT   provides topological specificity to cell division.";
RL   Mol. Microbiol. 7:601-610(1993).
RN   [4]
RP   STABILIZATION BY BOFA, AND POSSIBLE DEGRADATION BY FTSH.
RX   PubMed=10464210; DOI=10.1128/jb.181.17.5384-5388.1999;
RA   Resnekov O.;
RT   "Role of the sporulation protein BofA in regulating activation of the
RT   Bacillus subtilis developmental transcription factor sigmaK.";
RL   J. Bacteriol. 181:5384-5388(1999).
RN   [5]
RP   SUBUNIT.
RX   PubMed=11959848; DOI=10.1101/gad.977702;
RA   Rudner D.Z., Losick R.;
RT   "A sporulation membrane protein tethers the pro-sigmaK processing enzyme to
RT   its inhibitor and dictates its subcellular localization.";
RL   Genes Dev. 16:1007-1018(2002).
CC   -!- FUNCTION: Implicated in the coupling of mother cell to forespore gene
CC       expression. Required for spore formation at 37 degrees Celsius, but not
CC       at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining
CC       the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer
CC       forespore membrane. SpoIVFA brings BofA into close proximity to
CC       SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of
CC       SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the
CC       activation of sigma-K.
CC   -!- SUBUNIT: Forms a complex with BofA and SpoIVFB localized in the mother-
CC       cell membrane surrounding the forespore. {ECO:0000269|PubMed:11959848}.
CC   -!- INTERACTION:
CC       P26936; O35002: ctpB; NbExp=2; IntAct=EBI-5254757, EBI-5246793;
CC   -!- SUBCELLULAR LOCATION: Forespore outer membrane.
CC   -!- DEVELOPMENTAL STAGE: Transcribed during the stage II, but not required
CC       until stage IV of sporulation.
CC   -!- PTM: May be degraded by FtsH. It is stabilized by an ftsH disruption
CC       mutant, and in a probably independent fashion, by overexpression of
CC       BofA.
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DR   EMBL; X59528; CAA42106.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14758.1; -; Genomic_DNA.
DR   EMBL; Z15113; CAA78819.1; -; Genomic_DNA.
DR   PIR; S18437; S18437.
DR   RefSeq; NP_390676.1; NC_000964.3.
DR   RefSeq; WP_004398684.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P26936; -.
DR   SMR; P26936; -.
DR   IntAct; P26936; 3.
DR   STRING; 224308.BSU27980; -.
DR   PaxDb; P26936; -.
DR   PRIDE; P26936; -.
DR   EnsemblBacteria; CAB14758; CAB14758; BSU_27980.
DR   GeneID; 937501; -.
DR   KEGG; bsu:BSU27980; -.
DR   PATRIC; fig|224308.179.peg.3040; -.
DR   eggNOG; COG0739; Bacteria.
DR   OMA; MSHRADE; -.
DR   BioCyc; BSUB:BSU27980-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Sporulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..264
FT                   /note="Stage IV sporulation protein FA"
FT                   /id="PRO_0000072074"
FT   TOPO_DOM        1..72
FT                   /note="Mother cell cytoplasmic"
FT   TRANSMEM        73..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..264
FT                   /note="Forespore intermembrane space"
FT                   /evidence="ECO:0000305"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  29607 MW;  85723346B15932B6 CRC64;
     MSHRADEIRK RLEKRRKQLS GSKRFSTQTV SEKQKPPSWV MVTDQEKHGT LPVYEDNMPT
     FNGKHPLVKT DSIILKCLLS ACLVLVSAIA YKTNIGPVSQ IKPAVAKTFE TEFQFASASH
     WFETKFGNPL AFLAPEHKNK EQQIEVGKDL IAPASGKVQQ DFQDNGEGIK VETSSDKIDS
     VKEGYVVEVS KDSQTGLTVK VQHADNTYSI YGELKDVDVA LYDFVDKGKK LGSIKLDDHN
     KGVYYFAMKD GDKFIDPIQV ISFE