ID   MAMQ1_MAGSA             Reviewed;         272 AA.
AC   Q2W8P9;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Magnetosome protein MamQ 1 {ECO:0000305};
GN   Name=mamQ1; OrderedLocusNames=amb0972;
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, 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   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   [4]
RP   FUNCTION, 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: Essential for magnetosome formation (PubMed:20212111). Can be
CC       used to induce magnetosome formation (PubMed:26884433).
CC       {ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:26884433}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000250|UniProtKB:Q93DY8}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Part of the probable 18 gene mamAB operon.
CC       {ECO:0000305|PubMed:20212111}.
CC   -!- DISRUPTION PHENOTYPE: When both copies of this protein (amb0972 and
CC       amb1005) are deleted cells have no magnetic response and no magnetosome
CC       membranes. Deletion of just amb0972 leads to an intermediate magnetic
CC       response and still makes magnetosome membranes (PubMed:20212111). A
CC       careful electron cryotomography exam shows that in the double deletion
CC       empty vesicles that might be magnetosome precursors are present
CC       (PubMed:26884433). Deletion of genes mamH to mamV (amb0961 to amb0978)
CC       gives cells with no magnetosomes and no magnetic response
CC       (PubMed:20212111). {ECO:0000269|PubMed:20212111,
CC       ECO:0000269|PubMed:26884433}.
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   -!- MISCELLANEOUS: There is an identical gene in the genome (amb1005, AC
CC       Q2W8L6). {ECO:0000305|PubMed:16303747}.
CC   -!- SIMILARITY: Belongs to the LemA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE49776.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP007255; BAE49776.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2W8P9; -.
DR   SMR; Q2W8P9; -.
DR   EnsemblBacteria; BAE49776; BAE49776; amb0972.
DR   KEGG; mag:amb0972; -.
DR   HOGENOM; CLU_056714_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.
DR   Gene3D; 1.20.1440.20; -; 1.
DR   InterPro; IPR023353; LemA-like_dom_sf.
DR   InterPro; IPR007156; MamQ_LemA.
DR   PANTHER; PTHR34478; PTHR34478; 1.
DR   Pfam; PF04011; LemA; 1.
DR   SUPFAM; SSF140478; SSF140478; 1.
PE   3: Inferred from homology;
KW   Biomineralization; Magnetosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..272
FT                   /note="Magnetosome protein MamQ 1"
FT                   /id="PRO_0000447751"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..272
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   272 AA;  29948 MW;  EA34A2BD4A98198A CRC64;
     MALGDANVGS APGVDFSALQ RVKQSEELLA QLYVVEETPR RLGRGPVHAL MVISVLSVVA
     FIATLLMRYN TFVTMSEDTQ AKRSNYEVMI QRRDNLFGNL VKLTLNHAAL EHSIFSHTSD
     KRTEGVEAGK GGPIGSALEQ LMKQGGIGKL LGDIGGGKAL LGADGGFGNA LGRLMAVVEQ
     YPTIQSVDTY KHMMTSLVEM EDRIATRRED YNAAASTYNI EITKWPWNYL AFITGFKRAE
     YFQEKPAGDT PIITPQLFQE LLPLNHAQDI KK