ID   MMSF_MAGSA              Reviewed;         107 AA.
AC   Q2W8R4;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Magnetosome protein MmsF {ECO:0000305};
GN   Name=mmsF {ECO:0000303|PubMed:27481925}; OrderedLocusNames=amb0957;
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 [LARGE SCALE GENOMIC DNA].
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   [2]
RP   FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, AND
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   [3]
RP   SELF-ASSEMBLY, AND BIOTECHNOLOGY.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=25349410; DOI=10.1073/pnas.1409256111;
RA   Rawlings A.E., Bramble J.P., Walker R., Bain J., Galloway J.M.,
RA   Staniland S.S.;
RT   "Self-assembled MmsF proteinosomes control magnetite nanoparticle formation
RT   in vitro.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16094-16099(2014).
RN   [4]
RP   SUBCELLULAR LOCATION.
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   [5]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=26884433; DOI=10.1128/mbio.01898-15;
RA   Cornejo E., Subramanian P., Li Z., Jensen G.J., Komeili A.;
RT   "Dynamic Remodeling of the Magnetosome Membrane Is Triggered by the
RT   Initiation of Biomineralization.";
RL   MBio 7:E01898-E01898(2016).
CC   -!- FUNCTION: Plays a major role in synthesis of cubooctahedral magnetite
CC       crystals by controlling crystal growth and morphology after nucleation
CC       (PubMed:22716969). Has a partially redundant function with MamF (By
CC       similarity). When overexpressed in E.coli the soluble protein self
CC       assembles into shells of about 36 nm. This protein mediates the
CC       formation of magnetite nanoparticles from a solution of Fe(2+) and
CC       Fe(3+) sulfate; the crystals are larger and lack alternative iron
CC       oxide/oxyhydroxide species seen in the protein's absence
CC       (PubMed:25349410). {ECO:0000250|UniProtKB:A4U547,
CC       ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:25349410}.
CC   -!- ACTIVITY REGULATION: Its function may be negatively regulated by one of
CC       the MamGFDC proteins. {ECO:0000305|PubMed:22716969}.
CC   -!- SUBUNIT: May oligomerize. {ECO:0000305|PubMed:25349410}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:26884433,
CC       ECO:0000269|PubMed:27481925}; Multi-pass membrane protein {ECO:0000255,
CC       ECO:0000305|PubMed:22716969}. Note=Tagged protein forms straight lines
CC       with a punctate pattern extending along most of the cell associated
CC       with its inner curvature, in the correct position to be associated with
CC       magnetosomes (PubMed:22716969, PubMed:27481925, PubMed:26884433).
CC       During magnetosome formation protein is first dispersed in cell inner
CC       membrane, the gradually forms foci which align and form lines as the
CC       magnetic response increases (PubMed:26884433).
CC       {ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:26884433,
CC       ECO:0000269|PubMed:27481925}.
CC   -!- DISRUPTION PHENOTYPE: Single non-polar gene mutation and deletion of
CC       the probable mms6 operon (amb0955, mms6 and mmsF) leads to weak
CC       magnetic response and much smaller, elongated magnetite crystals
CC       (PubMed:22716969). Vesicles that are probably empty precursor
CC       magnetosomes are present and can grow to wild-type size
CC       (PubMed:26884433). {ECO:0000269|PubMed:22716969,
CC       ECO:0000269|PubMed:26884433}.
CC   -!- BIOTECHNOLOGY: May be useful for the manufacture of precision magnetite
CC       nanoparticles of uniform mineral type, and consistent morphology, with
CC       high magnetization. Addition to an Fe(2+) and Fe(3+) sulfate solution
CC       increases the quality of the magnetite crystals.
CC       {ECO:0000269|PubMed:25349410}.
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 MamF/MmsF protein family.
CC       {ECO:0000305}.
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DR   EMBL; AP007255; BAE49761.1; -; Genomic_DNA.
DR   RefSeq; WP_008620754.1; NC_007626.1.
DR   AlphaFoldDB; Q2W8R4; -.
DR   STRING; 342108.amb0957; -.
DR   EnsemblBacteria; BAE49761; BAE49761; amb0957.
DR   KEGG; mag:amb0957; -.
DR   HOGENOM; CLU_095018_0_1_5; -.
DR   OMA; FFSFSAM; -.
DR   OrthoDB; 1823639at2; -.
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.
PE   1: Evidence at protein level;
KW   Biomineralization; Magnetosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..107
FT                   /note="Magnetosome protein MmsF"
FT                   /id="PRO_0000447798"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:22716969"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..46
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..107
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   107 AA;  12039 MW;  B0C22B82032C9402 CRC64;
     MTEAILRSTL GARTTVMAAL SYLSVLCFVP LLVDRDDEFV YFHAKQGLVI WMWGVLALFA
     LHVPVLGKWI FGFSSMGVLV FSLLGLVSVV FQRAWKLPLI SWVAHRI