ID Q820N2_NITEU Unreviewed; 382 AA.
AC Q820N2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 ECO:0000313|EMBL:CAD84908.1};
GN OrderedLocusNames=NE0997 {ECO:0000313|EMBL:CAD84908.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD84908.1, ECO:0000313|Proteomes:UP000001416};
RN [1] {ECO:0000313|EMBL:CAD84908.1, ECO:0000313|Proteomes:UP000001416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC {ECO:0000313|Proteomes:UP000001416};
RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA Whittaker M., Arp D.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84908.1; -; Genomic_DNA.
DR RefSeq; WP_011111606.1; NC_004757.1.
DR AlphaFoldDB; Q820N2; -.
DR STRING; 228410.NE0997; -.
DR KEGG; neu:NE0997; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_2_4; -.
DR OrthoDB; 9813375at2; -.
DR PhylomeDB; Q820N2; -.
DR Proteomes; UP000001416; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 13..204
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 206..324
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT BINDING 108..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ SEQUENCE 382 AA; 40055 MW; 1A91735CFFEA92E3 CRC64;
MFEITNTEPL EAVIKVIGIG GCGGNAVDHM IRNEVKGVEF ICMNTDAQAL QGNRAQTLLQ
LGTSVTRGLG AGANPDIGKE AALEDRDHIA EIVQGADMLF ITAGMGGGTG TGAAPVVAQI
AKEMGILTVA VVSKPFSFEG KRLKAAQAGM EALAEHVDSL IVIPNDKLMK VLGNDISMLD
AFKAANDVLY GAVAGIAEVI NCPGLVNVDF ADVKTVMSEM GMAMMGSAAA SGVDRSRMAA
EEAVASPLLE EITLTGARGV LVNITASSAM KMREVQEVMD IVKKMTAEDA TVIVGTVIDE
NMGDSLRVTL VATGLGNINQ QSQRPMTVIH TRTGTDDRIS SHQVDEPAVM RTGRRSNAAV
TAMQQAGMDP MDIPAFLRRQ AD
//
