FTSZ_MYCTU
ID FTSZ_MYCTU Reviewed; 379 AA.
AC P9WN95; L0TBN4; O08378; P64170;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=Rv2150c;
GN ORFNames=MTCY270.18;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP RETRACTED PAPER.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066037; DOI=10.1371/journal.pone.0008590;
RA Sureka K., Hossain T., Mukherjee P., Chatterjee P., Datta P., Kundu M.,
RA Basu J.;
RT "Novel role of phosphorylation-dependent interaction between FtsZ and FipA
RT in mycobacterial cell division.";
RL PLoS ONE 5:E8590-E8590(2010).
RN [3]
RP RETRACTION NOTICE OF PUBMED:20066037.
RX PubMed=35202441; DOI=10.1371/journal.pone.0264672;
RG PLOS ONE Editors;
RL PLoS ONE 17:e0264672-e0264672(2022).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH GDP, AND SUBUNIT.
RX PubMed=15342249; DOI=10.1016/j.jmb.2004.07.061;
RA Leung A.K., Lucile White E., Ross L.J., Reynolds R.C., DeVito J.A.,
RA Borhani D.W.;
RT "Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G
RT protein-like conformational switches.";
RL J. Mol. Biol. 342:953-970(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, GTPASE
RP ACTIVITY, AND MUTAGENESIS OF ASP-210.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18479968; DOI=10.1016/j.tube.2008.03.001;
RA Respicio L., Nair P.A., Huang Q., Anil B., Tracz S., Truglio J.J.,
RA Kisker C., Raleigh D.P., Ojima I., Knudson D.L., Tonge P.J., Slayden R.A.;
RT "Characterizing septum inhibition in Mycobacterium tuberculosis for novel
RT drug discovery.";
RL Tuberculosis 88:420-429(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) IN COMPLEX WITH GDP, SUBUNIT, AND
RP MUTAGENESIS OF PHE-135; GLY-137; LYS-138; ASP-164; LEU-176; ALA-179;
RP LEU-203; ILE-204; LEU-269; ILE-289 AND PHE-291.
RX PubMed=23888039; DOI=10.1126/science.1239248;
RA Li Y., Hsin J., Zhao L., Cheng Y., Shang W., Huang K.C., Wang H.W., Ye S.;
RT "FtsZ protofilaments use a hinge-opening mechanism for constrictive force
RT generation.";
RL Science 341:392-395(2013).
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 (PubMed:15342249, PubMed:23888039). Polymerizes to
CC form a dynamic ring structure in a strictly GTP-dependent manner.
CC Interacts directly with several other division proteins (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039}.
CC -!- INTERACTION:
CC P9WN95; P9WP57: crgA; NbExp=5; IntAct=EBI-6414519, EBI-6414478;
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 -!- CAUTION: The article by Sureka et al was retracted by the editors after
CC publication. Concerns were raised regarding the results presented in
CC multiple figure panels. The raw data or replacement panels that were
CC available did not satisfactorily address all the issues, thus
CC questioning the integrity of the data. {ECO:0000305|PubMed:35202441}.
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DR EMBL; AL123456; CCP44926.1; -; Genomic_DNA.
DR PIR; B70579; B70579.
DR RefSeq; NP_216666.1; NC_000962.3.
DR RefSeq; WP_003411144.1; NZ_NVQJ01000044.1.
DR PDB; 1RLU; X-ray; 2.08 A; A/B=1-379.
DR PDB; 1RQ2; X-ray; 1.86 A; A/B=1-379.
DR PDB; 1RQ7; X-ray; 2.60 A; A/B=1-379.
DR PDB; 2Q1X; X-ray; 2.35 A; A/B=1-379.
DR PDB; 2Q1Y; X-ray; 2.30 A; A/B=1-379.
DR PDB; 4KWE; X-ray; 2.91 A; A/B/C=1-379.
DR PDB; 5V68; X-ray; 3.46 A; A/B/C/D/E/F=1-379.
DR PDB; 5ZUE; X-ray; 2.70 A; A=1-379.
DR PDBsum; 1RLU; -.
DR PDBsum; 1RQ2; -.
DR PDBsum; 1RQ7; -.
DR PDBsum; 2Q1X; -.
DR PDBsum; 2Q1Y; -.
DR PDBsum; 4KWE; -.
DR PDBsum; 5V68; -.
DR PDBsum; 5ZUE; -.
DR AlphaFoldDB; P9WN95; -.
DR SMR; P9WN95; -.
DR IntAct; P9WN95; 1.
DR STRING; 83332.Rv2150c; -.
DR BindingDB; P9WN95; -.
DR ChEMBL; CHEMBL4213; -.
DR DrugBank; DB01864; 5'-Guanosine-Diphosphate-Monothiophosphate.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR iPTMnet; P9WN95; -.
DR PaxDb; P9WN95; -.
DR DNASU; 888369; -.
DR GeneID; 45426128; -.
DR GeneID; 888369; -.
DR KEGG; mtu:Rv2150c; -.
DR TubercuList; Rv2150c; -.
DR eggNOG; COG0206; Bacteria.
DR OMA; GNPSIGQ; -.
DR PhylomeDB; P9WN95; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
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:0045787; P:positive regulation of cell cycle; IMP:MTBBASE.
DR GO; GO:0051258; P:protein polymerization; IDA:MTBBASE.
DR GO; GO:0000921; P:septin ring assembly; IMP:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..379
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114365"
FT BINDING 18..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039"
FT BINDING 105..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039"
FT BINDING 136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039"
FT BINDING 140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15342249, ECO:0000269|PubMed:23888039"
FT MUTAGEN 135
FT /note="F->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 137
FT /note="G->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 138
FT /note="K->A: Decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 164
FT /note="D->A: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 176
FT /note="L->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 179
FT /note="A->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 203
FT /note="L->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 204
FT /note="I->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 210
FT /note="D->G: Reduces FtsZ polymerization and GTP
FT hydrolysis. Does not affect the structure or the stability
FT of the unpolymerized FtsZ."
FT /evidence="ECO:0000269|PubMed:18479968"
FT MUTAGEN 269
FT /note="L->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 289
FT /note="I->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT MUTAGEN 291
FT /note="F->E: Strong decrease in GTPase activity."
FT /evidence="ECO:0000269|PubMed:23888039"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1RQ2"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5ZUE"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5ZUE"
FT HELIX 176..199
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 219..230
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:1RQ2"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1RQ2"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:1RQ2"
SQ SEQUENCE 379 AA; 38756 MW; 3F580353078788A9 CRC64;
MTPPHNYLAV IKVVGIGGGG VNAVNRMIEQ GLKGVEFIAI NTDAQALLMS DADVKLDVGR
DSTRGLGAGA DPEVGRKAAE DAKDEIEELL RGADMVFVTA GEGGGTGTGG APVVASIARK
LGALTVGVVT RPFSFEGKRR SNQAENGIAA LRESCDTLIV IPNDRLLQMG DAAVSLMDAF
RSADEVLLNG VQGITDLITT PGLINVDFAD VKGIMSGAGT ALMGIGSARG EGRSLKAAEI
AINSPLLEAS MEGAQGVLMS IAGGSDLGLF EINEAASLVQ DAAHPDANII FGTVIDDSLG
DEVRVTVIAA GFDVSGPGRK PVMGETGGAH RIESAKAGKL TSTLFEPVDA VSVPLHTNGA
TLSIGGDDDD VDVPPFMRR
