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Database: UniProt
Entry: V6KQE1_9ACTN
LinkDB: V6KQE1_9ACTN
Original site: V6KQE1_9ACTN 
ID   V6KQE1_9ACTN            Unreviewed;       366 AA.
AC   V6KQE1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE   Flags: Fragment;
GN   ORFNames=N566_18615 {ECO:0000313|EMBL:EST34317.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST34317.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST34317.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST34317.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) 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|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}.
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:EST34317.1}.
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DR   EMBL; AWQV01000627; EST34317.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6KQE1; -.
DR   STRING; 1380770.N566_18615; -.
DR   HOGENOM; CLU_024865_0_1_11; -.
DR   OrthoDB; 9813375at2; -.
DR   Proteomes; UP000017915; 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; 3.30.1330.20; 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|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU000631};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618,
KW   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017915};
KW   Septation {ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          10..202
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          204..321
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          312..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         366
FT                   /evidence="ECO:0000313|EMBL:EST34317.1"
SQ   SEQUENCE   366 AA;  37574 MW;  FD144CE4E941C83B CRC64;
     MAAPQNYLAV IKVVGIGGGG VNAINRMIEV GLKGVEFIAI NTDAQALLMS DADVKLDVGR
     ELTRGLGAGA NPDVGRKAAE DHREEIEEVL KGADMVFVTA GEGGGTGTGG APVVANIARS
     LGALTIGVVT RPFTFEGRRR ANQAEDGIAG LRDEVDTLIV IPNDRLLSIS DRQVSVLDAF
     KSADQVLLSG VQGITDLITT PGLINLDFAD VKSVMSEAGS ALMGIGSARG DDRAVAAAEM
     AISSPLLEAS IDGARGVLLS ISGGSDLGLF EINEAAQLVS EAAHPEANII FGAVIDDALG
     DEVRVTVIAA GFDGGQPPPK NRDKVLGAYG SRDDSSPASR QADDTGDRST LGVLGPRDEE
     VPVPET
//
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