ID   MAMG_MAGSA              Reviewed;         103 AA.
AC   Q2W8R7;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Magnetosome protein MamG {ECO:0000305};
GN   Name=mamG; OrderedLocusNames=amb0954;
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   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).
CC   -!- FUNCTION: Plays a role in regulating magnetite crystal size.
CC       {ECO:0000250|UniProtKB:Q6NE75}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000250|UniProtKB:Q6NE75}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the probable mamGFDC operon leads to
CC       a slight reduction in magnetic response and slightly narrower magnetite
CC       crystals. {ECO:0000269|PubMed:22716969}.
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 MamG (TC 9.B.95) protein family.
CC       {ECO:0000305}.
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DR   EMBL; AP007255; BAE49758.1; -; Genomic_DNA.
DR   RefSeq; WP_008620749.1; NC_007626.1.
DR   AlphaFoldDB; Q2W8R7; -.
DR   EnsemblBacteria; BAE49758; BAE49758; amb0954.
DR   KEGG; mag:amb0954; -.
DR   HOGENOM; CLU_2260352_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; ISS:UniProtKB.
PE   3: Inferred from homology;
KW   Biomineralization; Magnetosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..103
FT                   /note="Magnetosome protein MamG"
FT                   /id="PRO_0000447800"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..59
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          60..67
FT                   /note="LG repeat"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   103 AA;  9269 MW;  6A61CA1C125B5828 CRC64;
     MAAQVGGQIL ANAAAPAKAS AAAGVGTGGA ALGVGSGIIA SPVGTAAIGN AMLTGKGVCL
     GLGLGLGAWG PVLVGIAGLA GAAYLVGKLK NCKAEVDAAA DAT