ID   MAMI_MAGSA              Reviewed;          69 AA.
AC   Q2W8Q9;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Magnetosome protein MamI {ECO:0000305};
GN   Name=mamI; OrderedLocusNames=amb0962;
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, SUBCELLULAR LOCATION, PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=20212111; DOI=10.1073/pnas.0914439107;
RA   Murat D., Quinlan A., Vali H., Komeili A.;
RT   "Comprehensive genetic dissection of the magnetosome gene island reveals
RT   the step-wise assembly of a prokaryotic organelle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:5593-5598(2010).
RN   [3]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=21883528; DOI=10.1111/j.1365-2958.2011.07815.x;
RA   Draper O., Byrne M.E., Li Z., Keyhani S., Barrozo J.C., Jensen G.,
RA   Komeili A.;
RT   "MamK, a bacterial actin, forms dynamic filaments in vivo that are
RT   regulated by the acidic proteins MamJ and LimJ.";
RL   Mol. Microbiol. 82:342-354(2011).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=21414040; DOI=10.1111/j.1365-2958.2011.07631.x;
RA   Quinlan A., Murat D., Vali H., Komeili A.;
RT   "The HtrA/DegP family protease MamE is a bifunctional protein with roles in
RT   magnetosome protein localization and magnetite biomineralization.";
RL   Mol. Microbiol. 80:1075-1087(2011).
RN   [5]
RP   MINIMAL MAGNETOSOME ISLAND.
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   [6]
RP   DOMAIN, BIOTECHNOLOGY, AND MAGNETITE-BINDING.
RX   PubMed=27528487; DOI=10.1002/cbic.201600377;
RA   Bereczk-Tompa E., Posfai M., Toth B., Vonderviszt F.;
RT   "Magnetite-binding flagellar filaments displaying the MamI loop motif.";
RL   ChemBioChem 17:2075-2082(2016).
RN   [7]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=28790202; DOI=10.1128/mbio.00679-17;
RA   Taoka A., Kiyokawa A., Uesugi C., Kikuchi Y., Oestreicher Z., Morii K.,
RA   Eguchi Y., Fukumori Y.;
RT   "Tethered Magnets Are the Key to Magnetotaxis: Direct Observations of
RT   Magnetospirillum magneticum AMB-1 Show that MamK Distributes Magnetosome
RT   Organelles Equally to Daughter Cells.";
RL   MBio 8:0-0(2017).
CC   -!- FUNCTION: Essential for magnetosome formation (PubMed:20212111). May
CC       bind magnetite (Probable). May be involved in an early stage of
CC       magnetosome nucleation (By similarity). {ECO:0000250|UniProtKB:Q6NE62,
CC       ECO:0000269|PubMed:20212111, ECO:0000305|PubMed:27528487}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000269|PubMed:28790202, ECO:0000305|PubMed:20212111}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=Tagged protein forms straight
CC       lines extending along most of the cell associated with its inner
CC       curvature, in the correct position to be associated with magnetosomes
CC       (PubMed:20212111, PubMed:21414040, PubMed:21883528, PubMed:28790202).
CC       In a mamK deletion MamI forms a linear punctate pattern, suggesting it
CC       is associated with magnetosomes (PubMed:20212111). In a mamE deletion
CC       MamI forms a linear punctate pattern (PubMed:21414040). In double
CC       mamJ/limJ deletion MamI forms a linear punctate pattern
CC       (PubMed:21883528). {ECO:0000269|PubMed:20212111,
CC       ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:21883528,
CC       ECO:0000269|PubMed:28790202}.
CC   -!- INDUCTION: Part of the probable 18 gene mamAB operon.
CC       {ECO:0000305|PubMed:20212111}.
CC   -!- DISRUPTION PHENOTYPE: Cells have no magnetic response and no
CC       magnetosome membranes (PubMed:20212111). Deletion of genes mamH to mamV
CC       (amb0961 to amb0978) gives cells with no magnetosomes and no magnetic
CC       response (PubMed:20212111). {ECO:0000269|PubMed:20212111}.
CC   -!- BIOTECHNOLOGY: A short loop (residues 21-31, which is probably in the
CC       magnetosome lumen) when inserted into a Salmonella flagellin protein
CC       (FliC) binds magnetite, which may be used to purify particular forms of
CC       magnetite. {ECO:0000269|PubMed:27528487}.
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   -!- MISCELLANEOUS: Expression of just the minimal mamAB gene cluster
CC       (amb0961 to amb0978), including this gene, is sufficient to form a
CC       minimal magnetosome chain with small magnetite particles.
CC       {ECO:0000269|PubMed:22716969}.
CC   -!- SIMILARITY: Belongs to the magnetosome MamI protein family.
CC       {ECO:0000305}.
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DR   EMBL; AP007255; BAE49766.1; -; Genomic_DNA.
DR   RefSeq; WP_008620768.1; NC_007626.1.
DR   AlphaFoldDB; Q2W8Q9; -.
DR   SMR; Q2W8Q9; -.
DR   EnsemblBacteria; BAE49766; BAE49766; amb0962.
DR   KEGG; mag:amb0962; -.
DR   HOGENOM; CLU_2788987_0_0_5; -.
DR   OMA; WSVVEFL; -.
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; Iron; Magnetosome; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..69
FT                   /note="Magnetosome protein MamI"
FT                   /id="PRO_0000447802"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..31
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:27528487"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   69 AA;  7158 MW;  F9684616256FEB07 CRC64;
     MPSVIFGLLA LALGLLGVTA WWWSVTEFLR GAVPVALLIL GLVALASGVQ SVRLPRSNKG
     TASDPDIDG