MAMM_MAGSA
ID MAMM_MAGSA Reviewed; 318 AA.
AC Q2W8Q4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Magnetosome protein MamM {ECO:0000305};
DE AltName: Full=Probable iron transporter MamM {ECO:0000305};
GN Name=mamM; OrderedLocusNames=amb0967;
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).
CC -!- FUNCTION: Probably plays a role in biomineralization (Probable).
CC Required for stable accumulation of MamB (By similarity). Probably
CC binds and transports iron. May nucleate iron crystal formation (By
CC similarity). {ECO:0000250|UniProtKB:V6F235,
CC ECO:0000305|PubMed:20212111}.
CC -!- SUBUNIT: Forms homodimers via its C-terminal domain (CTD) in the
CC presence of metal cations (By similarity). Interacts with MamB via
CC their CTD (By similarity). {ECO:0000250|UniProtKB:V6F235}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000250|UniProtKB:V6F235}; Multi-pass membrane protein
CC {ECO:0000255}. Cell inner membrane {ECO:0000250|UniProtKB:V6F235};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Part of the probable 18 gene mamAB operon.
CC {ECO:0000305|PubMed:20212111}.
CC -!- DOMAIN: The C-terminal domain (CTD) is probably responsible for
CC hetero- and homodimerization; it assumes a V-shaped, dimeric metallo-
CC chaperone-like fold that can open and close. Binds up to 3 divalent
CC metal cations (probably iron in vivo); upon binding there is a
CC conformational shift to a tighter dimer.
CC {ECO:0000250|UniProtKB:V6F235}.
CC -!- DISRUPTION PHENOTYPE: Cells have no magnetic response but still make
CC empty magnetosome membranes; magnetosome proteins MamA and MamE
CC localize normally (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 -!- 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 cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. {ECO:0000305}.
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DR EMBL; AP007255; BAE49771.1; -; Genomic_DNA.
DR RefSeq; WP_011383399.1; NC_007626.1.
DR AlphaFoldDB; Q2W8Q4; -.
DR SMR; Q2W8Q4; -.
DR EnsemblBacteria; BAE49771; BAE49771; amb0967.
DR KEGG; mag:amb0967; -.
DR HOGENOM; CLU_013430_3_6_5; -.
DR OMA; VHIRMEN; -.
DR OrthoDB; 381612at2; -.
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 GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1510.10; -; 1.
DR Gene3D; 3.30.70.1350; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027470; Cation_efflux_CTD.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR Pfam; PF16916; ZT_dimer; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 3: Inferred from homology;
KW Biomineralization; Cell inner membrane; Cell membrane; Ion transport; Iron;
KW Iron transport; Magnetosome; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..318
FT /note="Magnetosome protein MamM"
FT /id="PRO_0000447740"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..210
FT /note="Transmembrane domain (TMD)"
FT /evidence="ECO:0000305"
FT REGION 211..318
FT /note="C-terminal domain (CTD)"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:V6F235"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:V6F235"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:V6F235"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:V6F235"
SQ SEQUENCE 318 AA; 34550 MW; 366AF7FED5A2C0CA CRC64;
MRKSGCTVCS RSIGWVGLAV NTVLMVMKAF VGLIGGSQAM LADAMYSLKD MLNALMVVIG
TTISSKPLDA EHPYGHGKVE FILSMVVSVV FIGLTGYLLV HAVQILLDES MHRTPHLIVL
WAALVSVGVN VAMYFYSRCV AIETNSPIIK TMAKHHHGDA TASGAVALGI IGAHYLNMPW
IDPAVALWET IDLLLLGKVV FMDAYRGLMD HTAGEAVQNR IVDTAERVPG VRGVIHLRAR
YVGQDIWADM IIGVDPEHTV EQAHDICEAV QAAVCGKMRR IESLHVSAEA REAGDTSKPT
FSEEPLTYDE VMLSKVDN
