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Database: UniProt
Entry: Q2LDF9_BARGR
LinkDB: Q2LDF9_BARGR
Original site: Q2LDF9_BARGR 
ID   Q2LDF9_BARGR            Unreviewed;        93 AA.
AC   Q2LDF9;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   03-MAY-2023, entry version 62.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE   Flags: Fragment;
GN   Name=ftsZ {ECO:0000313|EMBL:ABC69749.1};
OS   Bartonella grahamii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=33045 {ECO:0000313|EMBL:ABC69749.1};
RN   [1] {ECO:0000313|EMBL:ABC69749.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M09 {ECO:0000313|EMBL:ABC69749.1};
RA   Kirillov M., Markov A., Lopyrev I., Levitskiy S., Manuvera V.,
RA   Bashkirov V., Smirnov G., Kosoy M.;
RT   "Distribution of Bartonella among rodents in Moscow region, Russia.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein that forms a contractile ring
CC       structure (Z ring) at the future cell division site. The regulation of
CC       the ring assembly controls the timing and the location of cell
CC       division. One of the functions of the FtsZ ring is to recruit other
CC       cell division proteins to the septum to produce a new cell wall between
CC       the dividing cells. Binds GTP and shows GTPase activity.
CC       {ECO:0000256|RuleBase:RU000631}.
CC   -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC       strictly GTP-dependent manner. {ECO:0000256|RuleBase:RU000631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000631}.
CC   -!- SIMILARITY: Belongs to the FtsZ family.
CC       {ECO:0000256|RuleBase:RU000631}.
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DR   EMBL; DQ334260; ABC69749.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LDF9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR020805; Cell_div_FtsZ_CS.
DR   InterPro; IPR045061; FtsZ/CetZ.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR   PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|RuleBase:RU000631};
KW   Cell division {ECO:0000256|RuleBase:RU000631};
KW   GTP-binding {ECO:0000256|RuleBase:RU000631};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000631};
KW   Septation {ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          1..93
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABC69749.1"
FT   NON_TER         93
FT                   /evidence="ECO:0000313|EMBL:ABC69749.1"
SQ   SEQUENCE   93 AA;  9884 MW;  25C53438FB156630 CRC64;
     EIIDHLADSH MVFITAGMGG GTGTGAAPVV ARAAREKGIL TVGVVTKPFQ FEGARRMKTA
     ESGIEELQKS VDTLIVIPNQ NLFRIANDKT TFA
//
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