ID A0A1I1TU95_9BURK Unreviewed; 398 AA.
AC A0A1I1TU95;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216204_13044 {ECO:0000313|EMBL:SFD62221.1};
OS Massilia yuzhufengensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1164594 {ECO:0000313|EMBL:SFD62221.1, ECO:0000313|Proteomes:UP000198639};
RN [1] {ECO:0000313|EMBL:SFD62221.1, ECO:0000313|Proteomes:UP000198639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12041 {ECO:0000313|EMBL:SFD62221.1,
RC ECO:0000313|Proteomes:UP000198639};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00909}.
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DR EMBL; FOLD01000030; SFD62221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1TU95; -.
DR STRING; 1164594.SAMN05216204_13044; -.
DR OrthoDB; 9813375at2; -.
DR Proteomes; UP000198639; 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; 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 14..202
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 204..322
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT BINDING 22..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 106..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ SEQUENCE 398 AA; 41211 MW; 1B7ABC988D67D79B CRC64;
MEFDMVDNAA LGTVIKVVGV GGAGGNAVQH MINKGVSGVE FIAANTDAQA LAVSGANNII
QIGESGLGAG MRPEVGRQLA EQSRTRIEDA LRGAHMVFIA AGMGGGTGTG AAPIVAEVAK
SMGALTVAVV SKPFSYEGDK CMQVAEAGLE ELTKHVDSLI VILNEKLEDI YEDESMLDWM
KHADDVLNNA VAGIAEIINV PGHINVDFND VKTIMSEQGK AMMGTATAAG VDRARIAAEQ
AVASPLLDGI DLSGAKGVLV NVTASRGLKG KEIKEVMAAV RAFAAPDASI AQGIAYDDAM
GDEIRVTVVA TGLGKNKKMT LVQPQQMLKT GTYNAPVMAG SSAIAGGLAM GSASSDALGG
MKQPAVWRRE QASEQVQAMQ RNGVETYDIP AFLRKQAD
//
