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Database: UniProt
Entry: B8E321_DICTD
LinkDB: B8E321_DICTD
Original site: B8E321_DICTD 
ID   B8E321_DICTD            Unreviewed;       405 AA.
AC   B8E321;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN   Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN   OrderedLocusNames=Dtur_1243 {ECO:0000313|EMBL:ACK42521.1};
OS   Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC   Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC   Dictyoglomus.
OX   NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK42521.1, ECO:0000313|Proteomes:UP000007719};
RN   [1] {ECO:0000313|Proteomes:UP000007719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX   PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA   Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT   "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT   6724 reveals a specialized carbohydrate fermentor.";
RL   Front. Microbiol. 7:1979-1979(2016).
CC   -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC       Z ring. May serve as a membrane anchor for the Z ring.
CC       {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC   -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC       Rule:MF_02033}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02033}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}.
CC       Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to
CC       the membrane through a conserved C-terminal amphipathic helix.
CC       {ECO:0000256|HAMAP-Rule:MF_02033}.
CC   -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP-
CC       Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
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DR   EMBL; CP001251; ACK42521.1; -; Genomic_DNA.
DR   RefSeq; WP_012583603.1; NC_011661.1.
DR   RefSeq; YP_002353135.1; NC_011661.1.
DR   AlphaFoldDB; B8E321; -.
DR   STRING; 515635.Dtur_1243; -.
DR   EnsemblBacteria; ACK42521; ACK42521; Dtur_1243.
DR   KEGG; dtu:Dtur_1243; -.
DR   PATRIC; fig|515635.4.peg.1283; -.
DR   eggNOG; COG0849; Bacteria.
DR   HOGENOM; CLU_037850_3_2_0; -.
DR   InParanoid; B8E321; -.
DR   OrthoDB; 9810567at2; -.
DR   Proteomes; UP000007719; 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:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.110; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   HAMAP; MF_02033; FtsA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR020823; Cell_div_FtsA.
DR   InterPro; IPR003494; SHS2_FtsA.
DR   NCBIfam; TIGR01174; ftsA; 1.
DR   PANTHER; PTHR32432:SF4; CELL DIVISION PROTEIN FTSA; 1.
DR   PANTHER; PTHR32432; CELL DIVISION PROTEIN FTSA-RELATED; 1.
DR   Pfam; PF14450; FtsA; 1.
DR   Pfam; PF02491; SHS2_FTSA; 1.
DR   PIRSF; PIRSF003101; FtsA; 1.
DR   SMART; SM00842; FtsA; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02033};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02033}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02033};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007719}.
FT   DOMAIN          5..195
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   405 AA;  44863 MW;  ABC027F4D1C28703 CRC64;
     MSDFIGAIDL GSTKVAVVIA NLSEKNEELE LIGFSMIPSK GISYGVINDI QEASACIKEA
     VQRAVRMAGI RSIPKMIATI SGEKITAIPS RGMIIVKSRE QEVTESDVRR AIEAAKATSI
     PEDREVIYHV VRGFRLDGQN GIMNPIGMIG TRLESDLLLV THDKVQLRNI INAFQKAEIN
     IEGFIPQEIA ASEAVLTPEE KNLGVVLVDI GGDLTNLAVF KEGYLYAIGI LKLGGERITK
     DIAITLKIPT EEAERAKKII GTLKEEKEES LEVMSLQQKR IKINTSQVRE IIQPRVEEIL
     DFVLKKLEEL NSPIELIPGG IVITGGTALL DGLEEFAQEY LKVPVRVSRS LRVYNIFEEK
     DAVFYSSAVG ALERITRTVS TDESSKNFLD YLKEIFKNIF SPFKE
//
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