MMS6_MAGSA
ID MMS6_MAGSA Reviewed; 133 AA.
AC Q2W8R5; Q83VL7;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Magnetite biomineralization protein Mms6 {ECO:0000303|PubMed:21169637};
DE AltName: Full=Magnetosome protein Mms6 {ECO:0000305};
GN Name=mms6; OrderedLocusNames=amb0956;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 75-110, FUNCTION,
RP SUBCELLULAR LOCATION, POSSIBLE PROTEOLYSIS, AND FE(3+)-BINDING.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=12496282; DOI=10.1074/jbc.m211729200;
RA Arakaki A., Webb J., Matsunaga T.;
RT "A novel protein tightly bound to bacterial magnetic particles in
RT Magnetospirillum magneticum strain AMB-1.";
RL J. Biol. Chem. 278:8745-8750(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=21169637; DOI=10.1074/jbc.m110.183434;
RA Tanaka M., Mazuyama E., Arakaki A., Matsunaga T.;
RT "MMS6 protein regulates crystal morphology during nano-sized magnetite
RT biomineralization in vivo.";
RL J. Biol. Chem. 286:6386-6392(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=22716969; DOI=10.1111/j.1365-2958.2012.08132.x;
RA Murat D., Falahati V., Bertinetti L., Csencsits R., Koernig A., Downing K.,
RA Faivre D., Komeili A.;
RT "The magnetosome membrane protein, MmsF, is a major regulator of magnetite
RT biomineralization in Magnetospirillum magneticum AMB-1.";
RL Mol. Microbiol. 85:684-699(2012).
RN [5]
RP FUNCTION, SELF-ASSEMBLY, DOMAIN, FE(3+)-BINDING, AND MUTAGENESIS OF TRP-79;
RP 84-LEU--LEU-92; TRP-95; 113-LYS--ALA-133; 114-SER--ASP-130; ILE-117;
RP LEU-128; ALA-131; LEU-132 AND ALA-133.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=23857056; DOI=10.3390/ijms140714594;
RA Feng S., Wang L., Palo P., Liu X., Mallapragada S.K., Nilsen-Hamilton M.;
RT "Integrated self-assembly of the Mms6 magnetosome protein to form an iron-
RT responsive structure.";
RL Int. J. Mol. Sci. 14:14594-14606(2013).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=24961165; DOI=10.1111/mmi.12683;
RA Arakaki A., Yamagishi A., Fukuyo A., Tanaka M., Matsunaga T.;
RT "Co-ordinated functions of Mms proteins define the surface structure of
RT cubo-octahedral magnetite crystals in magnetotactic bacteria.";
RL Mol. Microbiol. 93:554-567(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27481925; DOI=10.1128/jb.00280-16;
RA Arakaki A., Kikuchi D., Tanaka M., Yamagishi A., Yoda T., Matsunaga T.;
RT "Comparative subcellular localization analysis of magnetosome proteins
RT reveals a unique localization behavior of Mms6 protein onto magnetite
RT crystals.";
RL J. Bacteriol. 198:2794-2802(2016).
RN [8]
RP 2 FORMS EXIST IN MAGNETOSOMES, INTERACTION WITH MAMA, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=28955887; DOI=10.1016/j.bbrep.2016.05.010;
RA Nguyen H.V., Suzuki E., Oestreicher Z., Minamide H., Endoh H., Fukumori Y.,
RA Taoka A.;
RT "A protein-protein interaction in magnetosomes: TPR protein MamA interacts
RT with an Mms6 protein.";
RL Biochem. Biophys. Rep. 7:39-44(2016).
RN [9]
RP FUNCTION, FE(2+)-BINDING, AND DOMAIN.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27112228; DOI=10.1002/chem.201600322;
RA Rawlings A.E., Bramble J.P., Hounslow A.M., Williamson M.P.,
RA Monnington A.E., Cooke D.J., Staniland S.S.;
RT "Ferrous Iron Binding Key to Mms6 Magnetite Biomineralisation: A
RT Mechanistic Study to understand Magnetite Formation Using pH Titration and
RT NMR Spectroscopy.";
RL Chemistry 22:7885-7894(2016).
RN [10]
RP FUNCTION, DOMAIN, AND MAGNETITE-BINDING.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=26970040; DOI=10.1016/j.jsb.2016.03.001;
RA Nudelman H., Tercedor C.V., Kolusheva S., Gonzalez T.P., Widdrat M.,
RA Grimberg N., Levi H., Nelkenbaum O., Davidov G., Faivre D.,
RA Jimenez-Lopez C., Zarivach R.;
RT "Structure-function studies of the magnetite-biomineralizing magnetosome-
RT associated protein MamC.";
RL J. Struct. Biol. 194:244-252(2016).
RN [11]
RP FUNCTION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27019707; DOI=10.1039/c5ra16469a;
RA Bird S.M., Rawlings A.E., Galloway J.M., Staniland S.S.;
RT "Using a biomimetic membrane surface experiment to investigate the activity
RT of the magnetite biomineralisation protein Mms6.";
RL RSC Adv. 6:7356-7363(2016).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 83-GLY--GLY-93; 94-ALA--MET-112; 113-ARG--ALA-133; 116-ASP--ASP-130;
RP ASP-116; GLU-118; 123-ASP--ALA-133; SER-122; GLU-127 AND ASP-130.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27759096; DOI=10.1038/srep35670;
RA Yamagishi A., Narumiya K., Tanaka M., Matsunaga T., Arakaki A.;
RT "Core amino acid residues in the morphology-regulating protein, Mms6, for
RT intracellular magnetite biomineralization.";
RL Sci. Rep. 6:35670-35670(2016).
RN [13]
RP BIOTECHNOLOGY.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=28051139; DOI=10.1038/srep39755;
RA Elfick A., Rischitor G., Mouras R., Azfer A., Lungaro L., Uhlarz M.,
RA Herrmannsdoerfer T., Lucocq J., Gamal W., Bagnaninchi P., Semple S.,
RA Salter D.M.;
RT "Biosynthesis of magnetic nanoparticles by human mesenchymal stem cells
RT following transfection with the magnetotactic bacterial gene mms6.";
RL Sci. Rep. 7:39755-39755(2017).
RN [14]
RP BIOTECHNOLOGY.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=30168058; DOI=10.1134/s1607672918040051;
RA Kotelnikova P.A., Shipunova V.O., Aghayeva U.F., Stremovskiy O.A.,
RA Nikitin M.P., Novikov I.A., Schulga A.A., Deyev S.M., Petrov R.V.;
RT "Synthesis of Magnetic Nanoparticles Stabilized by Magnetite-Binding
RT Protein for Targeted Delivery to Cancer Cells.";
RL Dokl. Biochem. Biophys. 481:198-200(2018).
RN [15]
RP FUNCTION, FE(2+)-BINDING, DOMAIN, AND MUTAGENESIS OF 123-ASP-GLU-124;
RP ASP-123 AND GLU-124.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=30405554; DOI=10.3389/fmicb.2018.02480;
RA Nudelman H., Lee Y.Z., Hung Y.L., Kolusheva S., Upcher A., Chen Y.C.,
RA Chen J.Y., Sue S.C., Zarivach R.;
RT "Understanding the biomineralization role of magnetite-interacting
RT components (MICs) from magnetotactic bacteria.";
RL Front. Microbiol. 9:2480-2480(2018).
CC -!- FUNCTION: Promotes the formation of magnetite in Fe(2+)-rich
CC conditions, when magnetite is not readily formed (PubMed:27112228).
CC Binds Fe(3+) and Fe(2+) (PubMed:12496282, PubMed:23857056,
CC PubMed:27112228) (Probable). May play a role in nucleation of magnetite
CC crystal formation (Probable) (PubMed:22716969). May help control
CC production of crystals with a specific morphology (Probable)
CC (PubMed:22716969, PubMed:27759096). Greatly improves the formation of
CC magnetosome-like magnetite crystals in vitro (PubMed:12496282).
CC Isolated short protein, probably residues 75-133, binds up to 18 Fe(3+)
CC per monomer and self-assembles into micelles about 21-26 nm in
CC diameter; the C-terminal 21 residues also self-assemble
CC (PubMed:23857056). {ECO:0000269|PubMed:12496282,
CC ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:23857056,
CC ECO:0000269|PubMed:27112228, ECO:0000269|PubMed:27759096,
CC ECO:0000305|PubMed:12496282, ECO:0000305|PubMed:21169637,
CC ECO:0000305|PubMed:26970040, ECO:0000305|PubMed:27019707,
CC ECO:0000305|PubMed:30405554}.
CC -!- SUBUNIT: Full length protein oligomerizes (PubMed:28955887). Full-
CC length protein interacts with MamA (PubMed:28955887).
CC {ECO:0000269|PubMed:28955887}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:16303747,
CC ECO:0000269|PubMed:27759096, ECO:0000269|PubMed:28955887}; Single-pass
CC membrane protein {ECO:0000255}. Note=Tightly associated with magnetite
CC crystals (PubMed:12496282). Tagged protein forms straight lines with a
CC punctate pattern extending along most of the cell associated with its
CC inner curvature, in the correct position to be associated with
CC magnetosomes. Under aerobic conditions, when magnetites cannot form, or
CC in the absence of iron, the protein is dispersed in the cell, probably
CC in the inner membrane; as magnetosomes form tagged Mms6 localizes in a
CC line that corresponds to the position of magnetite crystals
CC (PubMed:27481925). Short protein seems to localize specifically to
CC magnetosomes which have magnetite crystals (Probable).
CC {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:27481925,
CC ECO:0000305|PubMed:27481925}.
CC -!- DOMAIN: Fe(3+) binding by the shorter form (residues 75-133) is
CC inhibited by Ca(2+) and Mg(2+) (PubMed:12496282). The C-terminal 21
CC residues (magnetite-interacting component, MIC, residues 112-133) self
CC assemble into multimers up to octamers; this fragment binds Fe(3+)
CC which alters its structure (PubMed:23857056). Another paper showed
CC binding of MIC to Fe(2+) via Asp-123, Glu-124, Glu-125, and Glu-127
CC with a minor contribution from Glu-118 (PubMed:27112228). The isolated
CC lumenal MIC binds Fe(2+) and Ni(2+), Ni(2+)-binding may not be
CC physiological; in this paper binding to Fe(3+) was poor. Although it
CC binds iron the protein fragment has no effect on magnetite crystal
CC formation in an iron co-precipitation experiment, however mutating some
CC of its residues decreases crystal size (PubMed:30405554). Correct
CC subcellular location to the magnetosomes requires the N-terminal 75
CC residues (PubMed:27481925). {ECO:0000269|PubMed:12496282,
CC ECO:0000269|PubMed:23857056, ECO:0000269|PubMed:27112228,
CC ECO:0000269|PubMed:27481925, ECO:0000269|PubMed:30405554}.
CC -!- PTM: Seen in gels as a band of about 6 kDa which has residue 75 as its
CC N-terminus, suggesting it may undergo cleavage (Probable). 2 forms, a
CC full-length and the shorter protein are both detected immunologically
CC in magnetosomes (PubMed:28955887). {ECO:0000269|PubMed:28955887,
CC ECO:0000305|PubMed:12496282}.
CC -!- DISRUPTION PHENOTYPE: No effect on bacterial growth. Magnetosomes are
CC wild-type in number and size, but slightly less regularly spaced.
CC Magnetite crystals are smaller, irregularly shaped instead of
CC cubooctahedral, crystal growth may be incomplete. Magnetite-associated
CC proteins Mms5, MamC and MamD levels are significantly decreased
CC (PubMed:21169637). Single non-polar gene mutation has a slightly
CC reduced magnetic response, crystals are smaller and elongated
CC (PubMed:22716969, PubMed:27759096). Magnetite crystals are elongated
CC and their surface structure is altered, iron uptake is wild-type
CC (PubMed:24961165). Deletion of the probable mms6 operon (amb0955, mms6
CC and mmsF) leads to weak magnetic response and much smaller, elongated
CC magnetite crystals (PubMed:22716969). {ECO:0000269|PubMed:21169637,
CC ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:24961165,
CC ECO:0000269|PubMed:27759096}.
CC -!- BIOTECHNOLOGY: Transfection of a codon optimized gene into human
CC adipose-derived stem cells yields cells with magnetic crystals; the
CC crystals do not have a noticeable effect on cell proliferation,
CC migration or differentiation. {ECO:0000269|PubMed:28051139}.
CC -!- BIOTECHNOLOGY: A fusion of MIC to barstar (an RNase inhibitor from
CC B.amyloliquefaciens) binds and stabilizes coprecipitated magnetite
CC nanoparticles for at least 2 months. Cells transfected with barnase
CC (the ribonuclease target of barstar) can be specifically targeted by
CC magnetite-bound barstar which could be used in cell-specific cancer
CC treatment. {ECO:0000269|PubMed:30168058}.
CC -!- MISCELLANEOUS: This bacteria makes up to 20 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 magnetosome Mms6 family. {ECO:0000305}.
CC -!- CAUTION: PMID:21169637 identified the deleted gene as YP_420381.1
CC (equivalent to amb1018, mamY), which does not correspond to either the
CC gene or protein sequenced by the same authors. It is not clear which
CC gene was really deleted. {ECO:0000305|PubMed:21169637}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE49760.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB096081; BAC65162.1; -; Genomic_DNA.
DR EMBL; AP007255; BAE49760.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q2W8R5; -.
DR EnsemblBacteria; BAE49760; BAE49760; amb0956.
DR KEGG; mag:amb0956; -.
DR HOGENOM; CLU_1675763_0_0_5; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110146; C:magnetosome membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Biomineralization; Direct protein sequencing; Iron; Magnetosome; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..133
FT /note="Magnetite biomineralization protein Mms6"
FT /id="PRO_0000447815"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..133
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..75
FT /note="Required for localization to magnetosomes"
FT /evidence="ECO:0000269|PubMed:27481925"
FT REGION 83..92
FT /note="GL repeat"
FT /evidence="ECO:0000305"
FT REGION 112..133
FT /note="MIC, self-assembles, binds magnetite, Fe(2+) and
FT Fe(3+)"
FT /evidence="ECO:0000269|PubMed:23857056,
FT ECO:0000269|PubMed:26970040, ECO:0000269|PubMed:27112228,
FT ECO:0000269|PubMed:30405554"
FT MUTAGEN 79
FT /note="W->A: Self-assembly of the mature protein is
FT reduced."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 79
FT /note="W->F: No change in self-assembly of the mature
FT protein."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 83..93
FT /note="Missing: Makes rod shaped crystals; protein not in
FT magnetosome membranes."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 84..92
FT /note="LGLGLGLGL->AGAGAGAGA: Self-assembly of the mature
FT protein is reduced."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 94..112
FT /note="Missing: Makes rod shaped crystals."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 95
FT /note="W->A: Self-assembly of the mature protein is
FT reduced."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 95
FT /note="W->F: No change in self-assembly of the mature
FT protein."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 113..133
FT /note="KSRDIESAQSDEEVELRDALA->QSLERAEDEDADISAVEKLSR: Self-
FT assembly of the mature protein is reduced; isolated peptide
FT does not bind Fe(3+)."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 113..133
FT /note="Missing: Makes rod shaped crystals; protein not in
FT magnetosome membranes."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 114..130
FT /note="SRDIESAQSDEEVELRD->DRSIDEAQESDSVELRE: Self-assembly
FT of the mature protein is reduced; no longer binds Fe(3+)."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 116..130
FT /note="DIESAQSDEEVELRD->KIKSAQSKKKVKLKRK: Makes rod shaped
FT crystals."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 116
FT /note="D->A: Makes wild-type crystals; protein is in
FT magnetosome membrane."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 117
FT /note="I->G: No change in self-assembly of the mature
FT protein."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 118
FT /note="E->A: Makes wild-type crystals; protein is in
FT magnetosome membrane."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 122
FT /note="S->A: Makes wild-type crystals; protein is in
FT magnetosome membrane."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 123..133
FT /note="Missing: Makes rod shaped crystals."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 123..124
FT /note="DE->AA: Isolated MIC makes smaller magnetite
FT crystals."
FT /evidence="ECO:0000269|PubMed:30405554"
FT MUTAGEN 123
FT /note="D->A: Makes rod shaped crystals; protein is in
FT magnetosome membrane. Isolated MIC makes slightly smaller
FT magnetite crystals."
FT /evidence="ECO:0000269|PubMed:27759096,
FT ECO:0000269|PubMed:30405554"
FT MUTAGEN 124
FT /note="E->A: Makes rod shaped crystals; protein is in
FT magnetosome membrane. Isolated MIC makes wild-type size
FT magnetite crystals."
FT /evidence="ECO:0000269|PubMed:27759096,
FT ECO:0000269|PubMed:30405554"
FT MUTAGEN 125
FT /note="E->A: Makes rod shaped crystals; protein is in
FT magnetosome membrane."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 127
FT /note="E->A: Makes wild-type crystals; protein is in
FT magnetosome membrane."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 128
FT /note="L->G: Self-assembly of the mature protein is
FT reduced."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 130
FT /note="D->A: Makes wild-type crystals; protein is in
FT magnetosome membrane."
FT /evidence="ECO:0000269|PubMed:27759096"
FT MUTAGEN 131
FT /note="A->C: Mature protein forms a lattice."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 132
FT /note="L->G: Self-assembly of the mature protein is
FT significantly reduced."
FT /evidence="ECO:0000269|PubMed:23857056"
FT MUTAGEN 133
FT /note="A->C: Mature protein forms worm-like structures and
FT spheres."
FT /evidence="ECO:0000269|PubMed:23857056"
SQ SEQUENCE 133 AA; 12531 MW; F3FBB2048AB60D99 CRC64;
MGEMEREGAA AKAGAAKTGA AKTGTVAKTG IAAKTGVATA VAAPAAPANV AAAQGAGTKV
ALGAGKAAAG AKVVGGTIWT GKGLGLGLGL GLGAWGPIIL GVVGAGAVYA YMKSRDIESA
QSDEEVELRD ALA
