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Database: UniProt
Entry: F7K8I5_9FIRM
LinkDB: F7K8I5_9FIRM
Original site: F7K8I5_9FIRM 
ID   F7K8I5_9FIRM            Unreviewed;       397 AA.
AC   F7K8I5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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=HMPREF0994_02169 {ECO:0000313|EMBL:EGN41076.1};
OS   Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN41076.1, ECO:0000313|Proteomes:UP000003336};
RN   [1] {ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGN41076.1, ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN41076.1,
RC   ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1.";
RL   Submitted (APR-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|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: 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:EGN41076.1}.
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DR   EMBL; ACTP02000001; EGN41076.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7K8I5; -.
DR   STRING; 658086.HMPREF0994_02169; -.
DR   PATRIC; fig|658086.3.peg.2374; -.
DR   eggNOG; COG0206; Bacteria.
DR   HOGENOM; CLU_024865_0_2_9; -.
DR   Proteomes; UP000003336; 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; 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:UP000003336};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          14..206
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          208..323
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          326..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         109..111
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   397 AA;  41719 MW;  88171A9DDE5453C6 CRC64;
     MLEIKTNDAE SAAKIIVVGV GGAGNNAVNR MIDEKIDGVD FVGVNTDKQA LQLCKAPKLL
     QIGEKLTKGL GAGAKPEIGA KAAEESTDEI TNALTGSDMV FVTCGMGGGT GTGAAPVIAG
     IAKKMGILTV GVVTKPFRFE ARTRMTNALN GIERLKDSVD TLIVIPNDKL LEIVDRRTTM
     PEALKKADEV LQQAVQGITD LINVPAVINL DFADVQTVMK EKGIAHIGIG HGKGDDKASE
     AVKMAVESPL LETTIAGATD VIINVSGDIS MYDADDAASY VQQLTGDDVN IIFGAMYDDS
     TPDTCQITVI ATGLDDKPQQ AQNKFGSQFS VKPQQSPVKP VQPGMGTRPY TPVSPAPAAG
     TKPVAPAPNY TGIHKPGNLR SNVEEKSLKI PDFLQKK
//
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