FTSA_BACSU
ID FTSA_BACSU Reviewed; 440 AA.
AC P28264; Q45573;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; OrderedLocusNames=BSU15280;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3139638; DOI=10.1128/jb.170.10.4855-4864.1988;
RA Beall B., Lowe M., Lutkenhaus J.;
RT "Cloning and characterization of Bacillus subtilis homologs of Escherichia
RT coli cell division genes ftsZ and ftsA.";
RL J. Bacteriol. 170:4855-4864(1988).
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 SEQUENCE REVISION TO 12; 26; 112 AND 349-350.
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14, AND INDUCTION.
RC STRAIN=168 / JH642;
RX PubMed=1569582; DOI=10.1016/0022-2836(92)90463-t;
RA Gonzy-Treboul G., Karmazyn-Campelli C., Stragier P.;
RT "Developmental regulation of transcription of the Bacillus subtilis ftsAZ
RT operon.";
RL J. Mol. Biol. 224:967-979(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, AND INDUCTION.
RX PubMed=1624452; DOI=10.1128/jb.174.14.4647-4656.1992;
RA Gholamhoseinian A., Shen Z., Wu J.J., Piggot P.;
RT "Regulation of transcription of the cell division gene ftsA during
RT sporulation of Bacillus subtilis.";
RL J. Bacteriol. 174:4647-4656(1992).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11298280; DOI=10.1046/j.1365-2958.2001.02356.x;
RA Feucht A., Lucet I., Yudkin M.D., Errington J.;
RT "Cytological and biochemical characterization of the FtsA cell division
RT protein of Bacillus subtilis.";
RL Mol. Microbiol. 40:115-125(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH FTSZ.
RX PubMed=16159787; DOI=10.1128/jb.187.18.6536-6544.2005;
RA Jensen S.O., Thompson L.S., Harry E.J.;
RT "Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring
RT independent, and FtsA is required for efficient midcell Z-Ring assembly.";
RL J. Bacteriol. 187:6536-6544(2005).
CC -!- FUNCTION: Cell division protein that is required for the assembly of
CC the Z ring (PubMed:16159787). May serve as a membrane anchor for the Z
CC ring (By similarity). Binds and hydrolyzes ATP (PubMed:11298280). Also
CC involved in sporulation (Probable). {ECO:0000250|UniProtKB:P0ABH0,
CC ECO:0000269|PubMed:11298280, ECO:0000269|PubMed:16159787,
CC ECO:0000305|PubMed:1569582, ECO:0000305|PubMed:1624452}.
CC -!- SUBUNIT: Homodimer (PubMed:11298280). Interacts with FtsZ
CC (PubMed:16159787). {ECO:0000269|PubMed:11298280,
CC ECO:0000269|PubMed:16159787}.
CC -!- INTERACTION:
CC P28264; O34894: ezrA; NbExp=5; IntAct=EBI-2122615, EBI-1567579;
CC P28264; P17865: ftsZ; NbExp=7; IntAct=EBI-2122615, EBI-1569853;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0ABH0};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P0ABH0}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P0ABH0}. Note=Localizes to the Z ring in an
CC FtsZ-dependent manner (PubMed:11298280). In sporulating cells,
CC preferentially localizes to only one of the two potential polar
CC division sites (PubMed:11298280). Targeted to the membrane through a
CC conserved C-terminal amphipathic helix (By similarity).
CC {ECO:0000250|UniProtKB:P0ABH0, ECO:0000269|PubMed:11298280}.
CC -!- INDUCTION: Transcription is controlled by three promoters. Two of these
CC promoters, P1 and P3 are expressed mainly during vegetative growth. The
CC third one, P2, is up-regulated around the onset of sporulation.
CC {ECO:0000269|PubMed:1569582, ECO:0000269|PubMed:1624452}.
CC -!- MISCELLANEOUS: In B.subtilis, unlike the situation in E.coli, the role
CC of FtsA in the recruitment of other division proteins to the division
CC site appears to be an indirect one, through ensuring that FtsZ forms a
CC proper ring. {ECO:0000305|PubMed:16159787}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02033, ECO:0000305}.
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DR EMBL; M22630; AAA22456.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13401.2; -; Genomic_DNA.
DR EMBL; X66239; CAA46968.1; -; Genomic_DNA.
DR EMBL; S39431; AAD13818.1; -; Genomic_DNA.
DR PIR; I39847; I39847.
DR RefSeq; NP_389411.2; NC_000964.3.
DR RefSeq; WP_009967186.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P28264; -.
DR SMR; P28264; -.
DR IntAct; P28264; 25.
DR STRING; 224308.BSU15280; -.
DR jPOST; P28264; -.
DR PaxDb; P28264; -.
DR PRIDE; P28264; -.
DR EnsemblBacteria; CAB13401; CAB13401; BSU_15280.
DR GeneID; 936145; -.
DR KEGG; bsu:BSU15280; -.
DR PATRIC; fig|224308.179.peg.1666; -.
DR eggNOG; COG0849; Bacteria.
DR InParanoid; P28264; -.
DR OMA; DGIIRHT; -.
DR PhylomeDB; P28264; -.
DR BioCyc; BSUB:BSU15280-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:CACAO.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR HAMAP; MF_02033; FtsA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR020823; Cell_div_FtsA.
DR InterPro; IPR003494; SHS2_FtsA.
DR Pfam; PF02491; SHS2_FTSA; 1.
DR PIRSF; PIRSF003101; FtsA; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01174; ftsA; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome;
KW Sporulation.
FT CHAIN 1..440
FT /note="Cell division protein FtsA"
FT /id="PRO_0000062729"
FT REGION 396..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 12
FT /note="I -> L (in Ref. 1; AAA22456)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="D -> G (in Ref. 1; AAA22456)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="E -> A (in Ref. 1; AAA22456)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="AS -> QG (in Ref. 1; AAA22456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 48192 MW; 4BF656A8C71BF15A CRC64;
MNNNELYVSL DIGTSNTKVI VGEMTDDSLN IIGVGNVPSE GLKKGSIVDI DETVHSIRKA
FDQAERMVGF PLRKAIVGVN GNYINIQDTN GVVAVSSENK EIQVEDVRRV MEAAQVVSVP
HEQLIVDVIP KQFIVDGRDE ITDPKKMLGV RLEVEGTLIT GSKTILHNLL RCVERAGIEI
TDICLQPLAA GSAALSKDEK NLGVALIDIG GGSTTIAVFQ NGHLTSTRVI PLGGENITKD
ISIGLRTSTE EAERVKKQLG HAYYDEASED EIFEVTVIGT NQKQTFTQQE AANIIEARVE
EILEIVSEEL RSMGITDLPG GFVLTGGQAA MPGVMSLAQD VLQNNVRVAS PNYIGVRDPQ
YMTGVGLIQF ACRNARIQGR KIGFKMPEEA IQEIAVSSSE EQEQHHHQNE VQQRPKGKQK
TQAEHNKQSK MKKLLSMFWE
