ID   FTSZ_BARBA              Reviewed;         592 AA.
AC   O31314;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
DE   AltName: Full=75 kDa antigen;
GN   Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909};
OS   Bartonella bacilliformis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35686 / KC584 / NCTC 12139;
RX   PubMed=9226264; DOI=10.1128/jb.179.14.4545-4552.1997;
RA   Padmalayam I., Anderson B., Kron M., Kelly T., Baumstark B.;
RT   "The 75-kilodalton antigen of Bartonella bacilliformis is a structural
RT   homolog of the cell division protein ftsZ.";
RL   J. Bacteriol. 179:4545-4552(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kelly T.;
RL   Submitted (APR-1998) 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:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC       strictly GTP-dependent manner. Interacts directly with several other
CC       division proteins. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00909}.
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DR   EMBL; AY599560; AAT38536.1; -; Genomic_DNA.
DR   RefSeq; WP_005767417.1; NZ_LQWW01000013.1.
DR   AlphaFoldDB; O31314; -.
DR   SMR; O31314; -.
DR   OMA; MTINLHR; -.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-UniRule.
DR   CDD; cd02201; FtsZ_type1; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   HAMAP; MF_00909; FtsZ; 1.
DR   InterPro; IPR000158; Cell_div_FtsZ.
DR   InterPro; IPR017844; Cell_div_FtsZ_C.
DR   InterPro; IPR020805; Cell_div_FtsZ_CS.
DR   InterPro; IPR045061; FtsZ/CetZ.
DR   InterPro; IPR024757; FtsZ_C.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR30314; PTHR30314; 1.
DR   Pfam; PF12327; FtsZ_C; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   TIGRFAMs; TIGR00065; ftsZ; 1.
DR   TIGRFAMs; TIGR03483; FtsZ_alphas_C; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Septation.
FT   CHAIN           1..592
FT                   /note="Cell division protein FtsZ"
FT                   /id="PRO_0000114342"
FT   REGION          333..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         111..113
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         190
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   592 AA;  63503 MW;  C32007DADCD2D75B CRC64;
     MTINLHRPDI AELKPRITVF GVGGGGGNAV NNMINAGLQG VDFVVANTDA QALAMSKAER
     VIQLGAAVTE GLGAGALPEV GQAAADECID EIIDHLADSH MVFITAGMGG GTGTGAAPVV
     ARAAREKGIL TVGVVTKPFQ FEGARRMKTA EAGIEELQKS VDTLIVIPNQ NLFRIANEKT
     TFADAFAMAD QVLYSGVASI TDLMIKEGLI NLDFADVRSV MHEMGRAMMG TGEASGEGRA
     LAAAEAAIAN PLLDETSMCG ARGLLISITG GRDMTLFEVD EAANRIREEV DADANVIFGA
     IDDESLEGVI RVSVVATGID RLASDVVQPS HSKFQKSVSS VRKNDSGINQ TASHPQSSQL
     RSESMVETIE SLEVEVSQSQ PVEEMFSPKS QIFAKPTDTA STSSRSAATY PFGHGQSDIY
     GKISNASRIQ VNSIPQQSTA AAVSMEATAH VLSEMTNIVE QSEEKQAQIQ PYIAPARMPE
     LKDFSPFTHG QGIHSSGLEQ GPRSLWQRLK QSLTYREEIE PEARLEPAVK PLQNEESHIY
     NKNVQKVSSQ DSSVYAPHRS TKLQSRALQD QRAFVNEEDQ LEIPAFLRRQ AN