FTSZ_MAGGM
ID FTSZ_MAGGM Reviewed; 562 AA.
AC V6F5E5; G8GJE0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000303|PubMed:24272781};
GN OrderedLocusNames=MGMSRv2__2503;
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24272781; DOI=10.1128/jb.00804-13;
RA Mueller F.D., Raschdorf O., Nudelman H., Messerer M., Katzmann E.,
RA Plitzko J.M., Zarivach R., Schueler D.;
RT "The FtsZ-like protein FtsZm of Magnetospirillum gryphiswaldense likely
RT interacts with its generic homolog and is required for biomineralization
RT under nitrate deprivation.";
RL J. Bacteriol. 196:650-659(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24625872; DOI=10.1128/genomea.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:0-0(2014).
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 (By
CC similarity). Mild overexpression impairs cell division, leading to very
CC elongated cells. Isolated protein forms filaments and bundles in the
CC presence of GTP (PubMed:24272781). {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:24272781}.
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 FtsZ-like protein
CC (also called FtsZm) (Probable). {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000305|PubMed:24272781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24272781}.
CC Note=Assembles at midcell at the inner surface of the cytoplasmic
CC membrane (Probable). Upon mild overexpression during extended growth
CC additional foci appear, which are probably blocked division sites. Foci
CC colocalize with FtsZ-like protein (also called FtsZm)
CC (PubMed:24272781). {ECO:0000269|PubMed:24272781,
CC ECO:0000305|PubMed:24272781}.
CC -!- DISRUPTION PHENOTYPE: Essential; it cannot be disrupted. Although it
CC colocalizes with paralog FtsZ-like, the latter cannot replace it.
CC {ECO:0000269|PubMed:24272781}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; JN157806; AEO79972.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99718.1; -; Genomic_DNA.
DR RefSeq; WP_024080680.1; NZ_CP027526.1.
DR AlphaFoldDB; V6F5E5; -.
DR SMR; V6F5E5; -.
DR STRING; 1430440.MGMSRv2_2503; -.
DR EnsemblBacteria; CDK99718; CDK99718; MGMSRv2__2503.
DR KEGG; mgry:MSR1_38110; -.
DR KEGG; mgy:MGMSRv2__2503; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_5_2_5; -.
DR OrthoDB; 389990at2; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
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:0007017; P:microtubule-based process; IEA:InterPro.
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; IPR017975; Tubulin_CS.
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; PS01135; FTSZ_2; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Septation.
FT CHAIN 1..562
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000447776"
FT REGION 404..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..486
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:0000255|HAMAP-Rule:MF_00909"
FT BINDING 110..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 449
FT /note="D -> G (in Ref. 1; AEO79972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 59309 MW; 211322A23BAC8D87 CRC64;
MLNFLPGNPQ DLKPKITVIG VGGAGGNAVN NMIASRLEGV EFIVANTDAQ AINQSRTERR
VQLGTTVAQG LGAGSRPEIG RAAAEESLEE VIGQIAGANM VFITAGMGGG TGSGAAPVIA
RAARDHGILT VGVVTKPFHF EGAHRMRTAE GAIEELSQYV DTLIIIPNQN LFRVATERTT
FADAFKMADD VLYSGVRGVT DLMIMPGLIN LDFADIRTVM SEMGKAMMGT GEAEGDKRAI
EAAEAAISNP LLDDTSMKGA KGVLINITGG MDMTLFEVDE AANRIRDEVD PEANIIFGST
FDEKLNGKMR VSVVATGIAS EAAAQPKPTV VSLNTPQAQP QPRVAAGGTA GAGFRPAVVT
AQAAPAAAVA VAQAQPQMEA RTVAQPAPQP AHQPVVTAQV RVQPAAARPA QQPMAETFRP
DPQLRLDPVL ERPVPATTSL QADFRADPDM GHLSQAVSHI AETAQAAPQP QRQPEIQRQQ
APQPQRQPEP EARRSGGLFG LLRRPAAAQP APQPQRHEPA PMAQQPRQEP ARMGNMATRS
EPSVARAGED LDIPAFLRRQ AN
