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Database: UniProt
Entry: C4KCR8_THASP
LinkDB: C4KCR8_THASP
Original site: C4KCR8_THASP 
ID   C4KCR8_THASP            Unreviewed;       380 AA.
AC   C4KCR8; A0A5C7SF85;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN   Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909,
GN   ECO:0000313|EMBL:TXH81625.1};
GN   OrderedLocusNames=Tmz1t_3422 {ECO:0000313|EMBL:ACR02016.1};
GN   ORFNames=E6Q80_16920 {ECO:0000313|EMBL:TXH81625.1};
OS   Thauera aminoaromatica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=164330 {ECO:0000313|EMBL:ACR02016.1, ECO:0000313|Proteomes:UP000002186};
RN   [1] {ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR02016.1, ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|EMBL:ACR02016.1,
RC   ECO:0000313|Proteomes:UP000002186};
RX   PubMed=23407619; DOI=10.4056/sigs.2696029;
RA   Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA   Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA   Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT   "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL   Stand. Genomic Sci. 6:325-335(2012).
RN   [3] {ECO:0000313|EMBL:TXH81625.1, ECO:0000313|Proteomes:UP000321192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin_27_1 {ECO:0000313|EMBL:TXH81625.1};
RA   Stamps B.W., Spear J.R.;
RT   "Metagenome Assembled Genomes from an Advanced Water Purification
RT   Facility.";
RL   Submitted (SEP-2018) 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}.
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}.
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DR   EMBL; CP001281; ACR02016.1; -; Genomic_DNA.
DR   EMBL; SSFD01000271; TXH81625.1; -; Genomic_DNA.
DR   RefSeq; WP_004306274.1; NZ_SSFD01000271.1.
DR   AlphaFoldDB; C4KCR8; -.
DR   STRING; 85643.Tmz1t_3422; -.
DR   KEGG; tmz:Tmz1t_3422; -.
DR   eggNOG; COG0206; Bacteria.
DR   HOGENOM; CLU_024865_0_5_4; -.
DR   OrthoDB; 9813375at2; -.
DR   Proteomes; UP000002186; Chromosome.
DR   Proteomes; UP000321192; 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; 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.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000313|EMBL:ACR02016.1}; 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:UP000002186};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   DOMAIN          13..200
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          202..320
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   BINDING         21..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         105..107
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         182
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   380 AA;  39495 MW;  F7A70EF1D1EE8D13 CRC64;
     MFEIVEKEAT GTVIKVVGVG GAGGNAVDHM IREGVKGVHF ISANTDAQAL KRCLAPVKVQ
     LGITGLGAGS KPEAGRAAAQ ESRDAISAAL EGAHMVFITG GMGGGTGTGA APVVAEIAKE
     MGLLTVAVVT KPFDFENRIR VAESGIEELT RHVDSLIVVL NDKLLEVFGD DAGFEECFRS
     ADNVLRSAVG GIAEIINVPG LVNVDFQDVR TAMAEMGRAM MGSAEAAGMD RARIAAEQAA
     VSPLLEGTEL SGARCVLINI TASKSLKMSE VRDAVKTVQA FAAPEAFVKY GTVFDDTMED
     RIRITVVATG LGAPRAARQP VMQVVQGTGT YGPAMGGAVD VTNLDVPAVM RSGRRTTVEA
     MSTSGVGTYD IPAFLRRQAD
//
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