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Database: UniProt
Entry: A0A031LU18_9GAMM
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ID   A0A031LU18_9GAMM        Unreviewed;       392 AA.
AC   A0A031LU18;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631};
GN   Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN   ORFNames=CL42_05295 {ECO:0000313|EMBL:EZQ11321.1};
OS   Acinetobacter sp. Ver3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ11321.1, ECO:0000313|Proteomes:UP000023816};
RN   [1] {ECO:0000313|EMBL:EZQ11321.1, ECO:0000313|Proteomes:UP000023816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ver3 {ECO:0000313|EMBL:EZQ11321.1,
RC   ECO:0000313|Proteomes:UP000023816};
RA   Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT   "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT   isolated from a high altitude andean lake.";
RL   Submitted (MAR-2014) 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|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
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:0000256|HAMAP-Rule:MF_00909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000256|HAMAP-Rule:MF_00909}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|ARBA:ARBA00009690,
CC       ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EZQ11321.1}.
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DR   EMBL; JFYL01000011; EZQ11321.1; -; Genomic_DNA.
DR   RefSeq; WP_035265829.1; NZ_JFYL01000011.1.
DR   AlphaFoldDB; A0A031LU18; -.
DR   eggNOG; COG0206; Bacteria.
DR   Proteomes; UP000023816; Unassembled WGS sequence.
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; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   HAMAP; MF_00909; FtsZ; 1.
DR   InterPro; IPR000158; Cell_div_FtsZ.
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   NCBIfam; TIGR00065; ftsZ; 1.
DR   PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR   PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00909};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00909};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          19..210
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          212..331
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          338..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         114..116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         149
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         192
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   392 AA;  42137 MW;  29D50C8EDFA7A39F CRC64;
     MASFEFLEDE QTDNNGQARF TVFGVGGGGG NAVQHMVQSD IKGVKFVCAN TDKQALDRMN
     APFKIQLGQQ STRGLGAGAN PDVGQIAAEE SRELIRQHLE GADMVFVTAG MGGGTGTGAA
     PVVAEIAQEM GILTVGVVTT PFNFEGRRRQ RSAEKGIEEL EKHVDSLIII PNQRLLSVYG
     DISMQDAYRK ADDVLLNAVR SIFDLVVRPG HINLDFADLK TAMSTRGYAM MGEGKSSGPD
     RAEDAARLAI RSPLLDNVNI MNAKGVLINI TGGNDVTLRE TEIITDVVNQ IVDLDEGEVF
     FGTVFDPDAR DEIRVTVIAT GLTRNANETE VKRRAPVSVN PSVGGQAAAL DEDDVPAISK
     RQNQESVAPE PSAAPRSAPM SIQDYLKNQQ RK
//
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