ID   FTSE_BACSU              Reviewed;         228 AA.
AC   O34814; Q795D6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cell division ATP-binding protein FtsE;
GN   Name=ftsE; OrderedLocusNames=BSU35260;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT   subtilis.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION IN SPORULATION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=18573177; DOI=10.1111/j.1365-2958.2008.06340.x;
RA   Garti-Levi S., Hazan R., Kain J., Fujita M., Ben-Yehuda S.;
RT   "The FtsEX ABC transporter directs cellular differentiation in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 69:1018-1028(2008).
CC   -!- FUNCTION: Part of the ABC transporter FtsEX involved in sporulation.
CC       May act as an importer, possibly at the top of a hierarchical cascade
CC       leading to the correct temporal initiation of sporulation. Acts
CC       upstream of the histidine kinases KinA, KinB and KinC, the RapA
CC       phosphatase and the Spo0A sporulation protein.
CC       {ECO:0000269|PubMed:18573177}.
CC   -!- SUBUNIT: Interacts with FtsX. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18573177};
CC       Peripheral membrane protein {ECO:0000269|PubMed:18573177}. Note=Unlike
CC       the E.coli ortholog, localization is not restricted to division septa,
CC       nor is localization dependent on FtsZ.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene and ftsX, the next gene
CC       in the operon, delay sporulation onset, as a result of which they form
CC       a medial rather than polar septum at the onset of sporulation. This is
CC       presumably due to slower phosphorylation and activation of the spo0A
CC       transcriptional regulator. However, at later time points these cells
CC       undergo polar division and eventually form smaller than wild-type
CC       mature spores. {ECO:0000269|PubMed:18573177}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AF017113; AAC67262.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15543.1; -; Genomic_DNA.
DR   PIR; D69627; D69627.
DR   RefSeq; NP_391406.1; NC_000964.3.
DR   RefSeq; WP_003228039.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O34814; -.
DR   SMR; O34814; -.
DR   STRING; 224308.BSU35260; -.
DR   PaxDb; O34814; -.
DR   PRIDE; O34814; -.
DR   EnsemblBacteria; CAB15543; CAB15543; BSU_35260.
DR   GeneID; 936681; -.
DR   KEGG; bsu:BSU35260; -.
DR   PATRIC; fig|224308.179.peg.3816; -.
DR   eggNOG; COG2884; Bacteria.
DR   InParanoid; O34814; -.
DR   OMA; LPMYQRA; -.
DR   PhylomeDB; O34814; -.
DR   BioCyc; BSUB:BSU35260-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR   GO; GO:0090529; P:cell septum assembly; IMP:UniProtKB.
DR   GO; GO:0045881; P:positive regulation of sporulation resulting in formation of a cellular spore; IMP:UniProtKB.
DR   GO; GO:0070297; P:regulation of phosphorelay signal transduction system; IMP:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005286; Cell_div_FtsE_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02673; FtsE; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..228
FT                   /note="Cell division ATP-binding protein FtsE"
FT                   /id="PRO_0000380255"
FT   DOMAIN          2..227
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   228 AA;  25620 MW;  5D707CF5B6B96E4F CRC64;
     MIEMKEVYKA YPNGVKALNG ISVTIHPGEF VYVVGPSGAG KSTFIKMIYR EEKPTKGQIL
     INHKDLATIK EKEIPFVRRK IGVVFQDFKL LPKLTVFENV AFALEVIGEQ PSVIKKRVLE
     VLDLVQLKHK ARQFPDQLSG GEQQRVSIAR SIVNNPDVVI ADEPTGNLDP DTSWEVMKTL
     EEINNRGTTV VMATHNKEIV NTMKKRVIAI EDGIIVRDES RGEYGSYD