FTSZ_MYCTA
ID FTSZ_MYCTA Reviewed; 379 AA.
AC A5U4H7;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=MRA_2165;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP FUNCTION AS A GTPASE, ACTIVITY REGULATION, INTERACTION WITH PKNA, AND
RP PHOSPHORYLATION.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=17068335; DOI=10.1074/jbc.m607216200;
RA Thakur M., Chakraborti P.K.;
RT "GTPase activity of mycobacterial FtsZ is impaired due to its
RT transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA.";
RL J. Biol. Chem. 281:40107-40113(2006).
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 (By similarity). Binds GTP and shows GTPase
CC activity. {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:17068335}.
CC -!- ACTIVITY REGULATION: Phosphorylation affects GTPase activity as well as
CC polymerization ability. {ECO:0000269|PubMed:17068335}.
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 (By similarity). Interacts with PknA.
CC {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:17068335}.
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 -!- PTM: Phosphorylated by PknA. {ECO:0000269|PubMed:17068335}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; CP000611; ABQ73927.1; -; Genomic_DNA.
DR RefSeq; WP_003411144.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U4H7; -.
DR SMR; A5U4H7; -.
DR STRING; 419947.MRA_2165; -.
DR EnsemblBacteria; ABQ73927; ABQ73927; MRA_2165.
DR GeneID; 45426128; -.
DR KEGG; mra:MRA_2165; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_11; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR Proteomes; UP000001988; Chromosome.
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; -; 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 Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Septation.
FT CHAIN 1..379
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000419741"
FT BINDING 18..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 105..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
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
