ID Q19MD7_VIBAL Unreviewed; 381 AA.
AC Q19MD7;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 13-SEP-2023, entry version 71.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN Name=ftsZ {ECO:0000313|EMBL:ABF66033.1};
OS Vibrio alginolyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663 {ECO:0000313|EMBL:ABF66033.1};
RN [1] {ECO:0000313|EMBL:ABF66033.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-148 {ECO:0000313|EMBL:ABF66033.1};
RX PubMed=17172518; DOI=10.1099/jmm.0.46759-0;
RA Tracz D.M., Backhouse P.G., Olson A.B., McCrea J.K., Walsh J.A., Ng L.K.,
RA Gilmour M.W.;
RT "Rapid detection of Vibrio species using liquid microsphere arrays and
RT real-time PCR targeting the ftsZ locus.";
RL J. Med. Microbiol. 56:56-65(2007).
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. {ECO:0000256|ARBA:ARBA00009690,
CC ECO:0000256|RuleBase:RU000631}.
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DR EMBL; DQ520262; ABF66033.1; -; Genomic_DNA.
DR AlphaFoldDB; Q19MD7; -.
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 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|RuleBase:RU000631};
KW Cell division {ECO:0000256|RuleBase:RU000631};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000631};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000631}; Septation {ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 1..189
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 191..309
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 315..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABF66033.1"
FT NON_TER 381
FT /evidence="ECO:0000313|EMBL:ABF66033.1"
SQ SEQUENCE 381 AA; 39341 MW; FB537337B0C4E1DF CRC64;
VGVGGGGGNA VEHMVRESIE GVEFISVNTD AQALRKTSVG NVIQIGGDIT KGLGAGANPQ
VGRDAALEDR DRIKDSLTGA DMVFIAAGMG GGTGTGAAPV IAEVAKELGI LTVAVVTKPF
SFEGKKRLAF AEQGIDELSK HVDSLITIPN EKLLKVLGRG VTLLEAFASA NDVLKNAVQG
IAELITRPGM INVDFADVRT VMSEMGHAMM GSGIAKGEDR AEEAAEMAIS SPLLEDIDLA
GARGVLVNIT AGLDMRLDEF ETVGNTVKAF ASDNATVVIG TSLDPDMTDE IRVTVVATGI
GNEKKPDITL VAGGKAKVAP TPQAQPQQQA AATQAEEKPA QTLQNNQVQE KPQVTPQPTN
TAPSSPASSS QSSAAPKQEK E
//
