ID A0A1Q6Y5D0_9CHLR Unreviewed; 296 AA.
AC A0A1Q6Y5D0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN ORFNames=AUH05_18445 {ECO:0000313|EMBL:OLB32570.1};
OS Ktedonobacter sp. 13_2_20CM_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805233 {ECO:0000313|EMBL:OLB32570.1, ECO:0000313|Proteomes:UP000185646};
RN [1] {ECO:0000313|EMBL:OLB32570.1, ECO:0000313|Proteomes:UP000185646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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.
CC {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:OLB32570.1}.
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DR EMBL; MNDA01000521; OLB32570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6Y5D0; -.
DR Proteomes; UP000185646; Unassembled WGS sequence.
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; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR000158; Cell_div_FtsZ.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
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; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 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|RuleBase:RU000631};
KW Cell division {ECO:0000256|RuleBase:RU000631, ECO:0000313|EMBL:OLB32570.1};
KW GTP-binding {ECO:0000256|RuleBase:RU000631};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000631};
KW Septation {ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 85..277
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 296
FT /evidence="ECO:0000313|EMBL:OLB32570.1"
SQ SEQUENCE 296 AA; 31567 MW; 9637FE5C091FC9E6 CRC64;
MSHDNAFKRD IAPKQWAGKP ESRPADVYDE QEDQWAVLRH EVESEDAKRQ DERVRPGWNR
RDTEEDVLPT QSPLDALEQG LHHVDIVVAG VGGGGMNAVN RMISTRVRGV RFIAMNTDAQ
VLSLSEAQGR IYLGQHYTKG VGAGGNSGIG MRAATESAAE IRAALGEADL VFIAAGMGGG
TGTGAAPVVA SIAKKIGALT IGIVTLPFTF EGSRRRRIAE EGLAELSAEI DALITIPNDR
LLATTGQDHS LSDAFKLADE VLRQGVQGIA EVITVPGMIN VDFADVRSVL HEAGRA
//
