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Database: UniProt
Entry: A0A2N3PQN3_9PROT
LinkDB: A0A2N3PQN3_9PROT
Original site: A0A2N3PQN3_9PROT 
ID   A0A2N3PQN3_9PROT        Unreviewed;       564 AA.
AC   A0A2N3PQN3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CWS72_20405 {ECO:0000313|EMBL:PKU22694.1};
OS   Telmatospirillum siberiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Telmatospirillum.
OX   NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU22694.1, ECO:0000313|Proteomes:UP000233293};
RN   [1] {ECO:0000313|Proteomes:UP000233293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA   Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA   Pester M., Loy A.;
RT   "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT   acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT   cycling.";
RL   Submitted (DEC-2017) 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:PKU22694.1}.
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DR   EMBL; PIUM01000028; PKU22694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3PQN3; -.
DR   OrthoDB; 9813375at2; -.
DR   Proteomes; UP000233293; 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; 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:UP000233293};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          15..207
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          209..327
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   REGION          387..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         23..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         110..112
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   564 AA;  60296 MW;  CF72EE73D5E04B39 CRC64;
     MINFHPSNTG ELKPRITVIG VGGAGGNAVN NMIQSHLEGV EFIVANTDAQ AMAQSRTDRR
     IQLGSNVTQG LGAGARPDIG RAAAEETLDE IISQMQGSNM VFITAGMGGG TGTGAAPVIA
     RAAREHGILT VGVVTKPFNF EGQHRMRLAD SGIEELSQYV DTLIIIPNQN LFRIASERTT
     FADAFKMADD VLYSGVRGVT DLMIMPGLIN LDFADIRTVM SEMGKAMMGT GEAEGEKRAL
     EAAEAAINNP LLEDISMKGA RGVLINITGG LDMTLFEVDE AANRIRDEVD PDANIIFGST
     FDEKLEGKMR VSVVATGIES AEQTQTRPTL ISLVDQKRQP AAIQPAAKAA GLTLAERVAG
     TAPMFHGTAA IAQPDLEEEL DAAIGGPRQE DERYQSEPSL SVRSEPAPEP TYAPRAEAAP
     SQRMEPTMSV RHETPARAEP AQGSLHIESP APRMEPRADL RPSAPAASYA QVAQRAQADA
     AEPVPEQHRR SGFLNRLAGH VKTASHVHAS ATQPAHRPAA PEPQADRQQP VAQPTRISPA
     DRLPTSRNDE DLLEIPAFLR RQAN
//
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