FTSZL_MAGGM
ID FTSZL_MAGGM Reviewed; 323 AA.
AC Q3BK72; V6F261;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=FtsZ-like protein {ECO:0000303|PubMed:20023033};
DE EC=3.6.1.- {ECO:0000269|PubMed:20023033};
GN Name=ftsZ-like {ECO:0000303|PubMed:20023033};
GN Synonyms=ftsZm {ECO:0000303|PubMed:22043287};
GN OrderedLocusNames=MGMSRv2__2324; ORFNames=mgI560, MGR_4147;
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].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=16237001; DOI=10.1128/jb.187.21.7176-7184.2005;
RA Ullrich S., Kube M., Schuebbe S., Reinhardt R., Schueler D.;
RT "A hypervariable 130-kilobase genomic region of Magnetospirillum
RT gryphiswaldense comprises a magnetosome island which undergoes frequent
RT rearrangements during stationary growth.";
RL J. Bacteriol. 187:7176-7184(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=17449609; DOI=10.1128/jb.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(2007).
RN [3]
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).
RN [4]
RP GTPASE ACTIVITY, ATPASE ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=20023033; DOI=10.1128/jb.01292-09;
RA Ding Y., Li J., Liu J., Yang J., Jiang W., Tian J., Li Y., Pan Y., Li J.;
RT "Deletion of the ftsZ-like gene results in the production of
RT superparamagnetic magnetite magnetosomes in Magnetospirillum
RT gryphiswaldense.";
RL J. Bacteriol. 192:1097-1105(2010).
RN [5]
RP PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=22043287; DOI=10.1371/journal.pone.0025561;
RA Lohsse A., Ullrich S., Katzmann E., Borg S., Wanner G., Richter M.,
RA Voigt B., Schweder T., Schueler D.;
RT "Functional analysis of the magnetosome island in Magnetospirillum
RT gryphiswaldense: the mamAB operon is sufficient for magnetite
RT biomineralization.";
RL PLoS ONE 6:E25561-E25561(2011).
RN [6]
RP INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24020498; DOI=10.1186/1471-2180-13-203;
RA Yang J., Li S., Huang X., Li J., Li L., Pan Y., Li Y.;
RT "MamX encoded by the mamXY operon is involved in control of magnetosome
RT maturation in Magnetospirillum gryphiswaldense MSR-1.";
RL BMC Microbiol. 13:203-203(2013).
RN [7]
RP FUNCTION, FORMS FILAMENTS, SUBCELLULAR LOCATION, 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 [8]
RP POSSIBLE FUNCTION, PROBABLE INTERACTION WITH MAMX AND MAMY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=30367002; DOI=10.1128/aem.02394-18;
RA Wang Q., Wu S., Li X., Zhang T., Yang J., Wang X., Li F., Li Y., Peng Y.,
RA Li J.;
RT "Work Patterns of MamXY Proteins during Magnetosome Formation in
RT Magnetospirillum gryphiswaldense MSR-1.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
CC -!- FUNCTION: Required for synthesis of single-domain magnetite particles
CC and magnetosomes, especially in the absence of nitrate. Forms
CC filaments, which form bundles in the presence of GTP. Has both GTPase
CC and ATPase activity; GTPase is 2.5 time more efficient. Has no activity
CC on CTP or TTP (PubMed:20023033). May be involved in redox control for
CC magnetite crystallization (Probable). Mild overexpression causes cell
CC elongation (PubMed:24272781). May recruit other proteins (MamX, MamY
CC and MamZ and possibly Mms6) to a complex required for biomineralization
CC (Probable). {ECO:0000269|PubMed:20023033, ECO:0000269|PubMed:24272781,
CC ECO:0000305|PubMed:24272781, ECO:0000305|PubMed:30367002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:20023033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:20023033};
CC -!- SUBUNIT: Interacts with FtsZ (Probable). Probably interacts with MamX
CC and MamY (PubMed:30367002). {ECO:0000269|PubMed:30367002,
CC ECO:0000305|PubMed:24272781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30367002,
CC ECO:0000305|PubMed:24272781}. Note=Upon mild overexpression assembles
CC into foci at midcell and at cell poles, foci colocalize with FtsZ but
CC not with MamK filaments. Subcellular location is independent of other
CC magnetosome locus encoded proteins, but may depend on FtsZ
CC (PubMed:24272781). A similar construct shows a dispersed location at 6
CC hours post-induction and a dot-like distribution at 18 hours post-
CC induction (PubMed:30367002). {ECO:0000269|PubMed:24272781,
CC ECO:0000269|PubMed:30367002}.
CC -!- INDUCTION: Expressed in exponential phase, peaks about 18 hours
CC (PubMed:20023033, PubMed:24020498). Fourth gene in the 4 gene mamXY
CC operon (PubMed:20023033) (Probable). {ECO:0000269|PubMed:20023033,
CC ECO:0000269|PubMed:24020498, ECO:0000305|PubMed:22043287,
CC ECO:0000305|PubMed:24020498}.
CC -!- DISRUPTION PHENOTYPE: Not essential for cell growth. When grown in
CC NH(4)Cl medium loss of magnetic response. Magnetosomes are much smaller
CC with poorly defined morphology, poor crystallization and are
CC irregularly distributed with large gaps. They are wild-type in number,
CC are magnetite but predominantly superparamagnetic instead of single-
CC domain (PubMed:20023033). When grown in NO(3-), nitrate, single
CC deletion cells are nearly wild-type; in this study NH(4)Cl-grown single
CC deletion cells make a few wild-type magnetosomes in addition to poor
CC crystals in chains, i.e. the phenotype is not as extreme as in the
CC previous study (PubMed:24272781). Deletion of 4 consecutive genes
CC (mamY, mamX, mamZ, ftsZm) leads to cells with an intermediate magnetic
CC response where magnetosomes have short chains of nearly regularly
CC shaped, cubo-octahedral crystals flanked by small particles with poorly
CC defined morphologies (PubMed:22043287). {ECO:0000269|PubMed:20023033,
CC ECO:0000269|PubMed:22043287, ECO:0000269|PubMed:24272781}.
CC -!- MISCELLANEOUS: This bacteria makes up to 60 cubo-octahedral
CC magnetosomes of about 45 nm in diameter which contain membrane-bound
CC crystals of magnetite (Fe(3)O(4)). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; AM085146; CAJ30168.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78079.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99539.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3BK72; -.
DR SMR; Q3BK72; -.
DR STRING; 1430440.MGMSRv2_2324; -.
DR EnsemblBacteria; CDK99539; CDK99539; MGMSRv2__2324.
DR KEGG; mgy:MGMSRv2__2324; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_5; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0090529; P:cell septum assembly; IEA:UniProtKB-UniRule.
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; PS01134; FTSZ_1; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..323
FT /note="FtsZ-like protein"
FT /id="PRO_0000447777"
FT BINDING 27..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 114..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT CONFLICT 1..12
FT /note="Missing (in Ref. 3; CDK99539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 33686 MW; 9AFD3D7C65B186B8 CRC64;
MFGVEPISFC EDMTMIRPRI IVIGVGGAGG NAVNNMILSK IEGVEFIAAN TDAQALGLSL
ADRRIPLGGY VTKGLGAGSR PELGRSAAQE SIDDILTAID DANMVFITAG MGGGTGSGAA
PVIAQAARER GILTIGVVTK PFHFEGGHRM GTAEAAIEEL QHVVDTLIII PNQNLFRIAS
ERTTFIDAFK MADNVLNSGV RSVTDLVVKP GLINLDFADI RIVMSEMGKA IMGTGEAEGE
PRAVKAAEAA ISNPLLGDTS IAGAKGVLIN ITGGMDMTLF EVDEAANRIR TEVAPDANII
FGSTFDEKLD GKMRVSVVAT GIA
