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FTSZ2_HALSA
ID   FTSZ2_HALSA             Reviewed;         393 AA.
AC   P0DMR7; Q48290; Q9HSK0;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Cell division protein FtsZ 2 {ECO:0000255|HAMAP-Rule:MF_00909};
GN   Name=ftsZ2 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=VNG_0192G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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:0000255|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:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00909}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG18804.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG18804.1; ALT_INIT; Genomic_DNA.
DR   PIR; H84179; H84179.
DR   PIR; T44848; T44848.
DR   RefSeq; WP_012289116.1; NC_002607.1.
DR   AlphaFoldDB; P0DMR7; -.
DR   SMR; P0DMR7; -.
DR   STRING; 64091.VNG_0192G; -.
DR   PaxDb; P0DMR7; -.
DR   EnsemblBacteria; AAG18804; AAG18804; VNG_0192G.
DR   GeneID; 5952416; -.
DR   GeneID; 62885920; -.
DR   KEGG; hal:VNG_0192G; -.
DR   PATRIC; fig|64091.14.peg.141; -.
DR   HOGENOM; CLU_024865_0_1_2; -.
DR   OrthoDB; 41117at2157; -.
DR   PhylomeDB; P0DMR7; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IBA:GO_Central.
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; -; 1.
DR   Gene3D; 3.40.50.1440; -; 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   PANTHER; PTHR30314; PTHR30314; 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; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   TIGRFAMs; TIGR00065; ftsZ; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Reference proteome; Septation.
FT   CHAIN           1..393
FT                   /note="Cell division protein FtsZ 2"
FT                   /id="PRO_0000114399"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..44
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         127..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         158
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   393 AA;  41318 MW;  5C482EC36D0000EA CRC64;
     MQDIVQDALD NAEAEQREMD GDGDGDEFGD PRIVIVGCGG AGNNTVNRLY NIGVEGADTV
     AINTDKQHLK MIKADTKILV GKSLTNGLGA GGDPSMGERA TEMAQGTIKE VLGDADLVFV
     TAGMGGGTGT GAAPVVSKIA KEQGAIVVGM VSTPFNVERA RTVKAEEGLE KLREKADSII
     VLDNNRLLDY VPNLPIGKAF SVMDQIIAET VKGISETITQ PSLINLDYAD MTAIMNQGGV
     AVMLVGETQD KNKTNEVVKD AMNHPLLDVD YRGASGGLVH ITGGPDLTLK EAEGIADNIT
     ERLDASANVI WGARIQESYK GKVRVMAIMT GVQSAQVLGP STQKQADKSR RELQDVDSKQ
     RAADDAGAGG FGGAHSDGGQ DEVEQENGLD VIR
 
 
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