MAMD_MAGSA
ID MAMD_MAGSA Reviewed; 314 AA.
AC Q2W8R9; Q83VL8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Magnetosome protein MamD {ECO:0000305};
DE AltName: Full=Magnetosome protein Mms7 {ECO:0000303|PubMed:12496282};
GN Name=mamD; Synonyms=mms7 {ECO:0000303|PubMed:12496282};
GN OrderedLocusNames=amb0952;
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 259-283, SUBCELLULAR
RP LOCATION, AND POSSIBLE PROTEOLYSIS.
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 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 [4]
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 [5]
RP FUNCTION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=25775527; DOI=10.1073/pnas.1417614112;
RA Jones S.R., Wilson T.D., Brown M.E., Rahn-Lee L., Yu Y., Fredriksen L.L.,
RA Ozyamak E., Komeili A., Chang M.C.;
RT "Genetic and biochemical investigations of the role of MamP in redox
RT control of iron biomineralization in Magnetospirillum magneticum.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3904-3909(2015).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, POSSIBLE PROTEOLYSIS, DISRUPTION PHENOTYPE,
RP AND BIOTECHNOLOGY.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27417732; DOI=10.1038/srep29785;
RA Yamagishi A., Tanaka M., Lenders J.J., Thiesbrummel J., Sommerdijk N.A.,
RA Matsunaga T., Arakaki A.;
RT "Control of magnetite nanocrystal morphology in magnetotactic bacteria by
RT regulation of mms7 gene expression.";
RL Sci. Rep. 6:29785-29785(2016).
RN [7]
RP FUNCTION, IRON-BINDING, DOMAIN, AND MUTAGENESIS OF ASP-304 AND ASP-305.
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: Helps regulate magnetite crystal morphology, probably in a
CC single growth axis (PubMed:27417732). May help control oxido-reduction
CC reactions surrounding the crystal lattice of the forming magnetite
CC mineral (Probable). Probably binds Fe(2+), may play a role in
CC nucleation of magnetite crystal formation (Probable). Expression in a
CC deletion mutant restores growth of spherical (wild-type) magnetite
CC crystals. Increased protein levels allow crystal growth in the minor
CC axis but not increased numbers of crystals (PubMed:27417732).
CC {ECO:0000269|PubMed:27417732, ECO:0000305|PubMed:25775527,
CC ECO:0000305|PubMed:30405554}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:16303747,
CC ECO:0000269|PubMed:27417732}; Single-pass membrane protein
CC {ECO:0000255}. Note=Tightly associated with magnetite crystals
CC (PubMed:12496282). Upon overexpression small amounts of a larger (full-
CC length) protein is seen in the cell inner membrane (PubMed:27417732).
CC {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:27417732}.
CC -!- DOMAIN: The isolated charged lumenal magnetite-interacting component
CC (MIC, residues 298-314) binds Fe(2+) and Ni(2+); Ni(2+)-binding may not
CC be physiological. Although it binds iron the protein fragment has no
CC effect on magnetite crystal formation in an iron co-precipitation
CC experiment, however mutating some of its residues decreases crystal
CC size. {ECO:0000269|PubMed:30405554}.
CC -!- PTM: Seen in gels as a band of about 7 kDa, suggesting it may undergo
CC cleavage (Probable). Upon overexpression a larger (full-length) protein
CC is seen in the cell inner membrane (PubMed:27417732).
CC {ECO:0000269|PubMed:27417732, ECO:0000305|PubMed:12496282,
CC ECO:0000305|PubMed:27417732}.
CC -!- DISRUPTION PHENOTYPE: Magnetite crystals are elongated and their
CC surface structure is altered (PubMed:24961165). Another deletion
CC missing both mamD and a 25 kb region of the magnetsome island locus
CC (called SID25) gives dumbbell-shaped magnetite crystals
CC (PubMed:24961165, PubMed:27417732). Deletion of the probable mamGFDC
CC operon leads to a slight reduction in magnetic response and slightly
CC narrower magnetite crystals (PubMed:22716969).
CC {ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:24961165,
CC ECO:0000269|PubMed:27417732}.
CC -!- BIOTECHNOLOGY: Fine-tuning of the expression of this gene allows
CC regulation of crystal growth along the minor axis; this can be used as
CC an alternative way to synthesize magnetic crystals with a desired
CC shape. {ECO:0000269|PubMed:27417732}.
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 MamD/Mms5 family. {ECO:0000305}.
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DR EMBL; AB096081; BAC65161.1; -; Genomic_DNA.
DR EMBL; AP007255; BAE49756.1; -; Genomic_DNA.
DR RefSeq; WP_011383389.1; NC_007626.1.
DR AlphaFoldDB; Q2W8R9; -.
DR EnsemblBacteria; BAE49756; BAE49756; amb0952.
DR KEGG; mag:amb0952; -.
DR HOGENOM; CLU_815860_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..314
FT /note="Magnetosome protein MamD"
FT /id="PRO_0000447793"
FT TOPO_DOM 1..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..314
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:30405554"
FT REGION 261..270
FT /note="GL repeat"
FT /evidence="ECO:0000305"
FT REGION 298..314
FT /note="Magnetite-interacting component (MIC), binds Fe(2+)"
FT /evidence="ECO:0000269|PubMed:30405554"
FT MUTAGEN 304
FT /note="D->A: Isolated MIC makes smaller magnetite
FT crystals."
FT /evidence="ECO:0000269|PubMed:30405554"
FT MUTAGEN 305
FT /note="D->A: Isolated MIC makes smaller magnetite
FT crystals."
FT /evidence="ECO:0000269|PubMed:30405554"
SQ SEQUENCE 314 AA; 29902 MW; 67EA1E1F5F9A1A71 CRC64;
MQDLLLAKVE SAMQASQVSA LAGQTATVTK VSAATNLATI TPTAAGQAPI IVKLDATRQV
VELQALVGKT VMVGKTPAAI GGIGNWIALT PVTGAKAAAA ATGAGQLVMM KVEGTAAAVN
LPALAGKSFT IAQPPVAAGT KAAGMLYLNP VGGGDLIAIN VQNAATQTGG LVGKTFVVAP
SPVIGGTTGK FLVLKPLTAG AGKAVGGGAI AAKFIPAAVT GTGGAAAVGA GSASSLLTAG
AGTVTPITAA GTGSAMLSAK GLGLGLGLGL GAWGPFLLGA AGLAGAAALY VWARRRHGTP
DLSDDALLAA AGEE
