MAMT_MAGSA
ID MAMT_MAGSA Reviewed; 176 AA.
AC Q2W8P5;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Magnetosome protein MamT {ECO:0000305};
DE AltName: Full=Magnetochrome MamT {ECO:0000305};
GN Name=mamT; OrderedLocusNames=amb0976;
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 POSSIBLE COFACTOR.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=23176475; DOI=10.1042/bst20120104;
RA Siponen M.I., Adryanczyk G., Ginet N., Arnoux P., Pignol D.;
RT "Magnetochrome: a c-type cytochrome domain specific to magnetotatic
RT bacteria.";
RL Biochem. Soc. Trans. 40:1319-1323(2012).
RN [4]
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 [5]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 103-CYS--HIS-107 AND
RP 154-CYS--HIS-158.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=25775527; DOI=10.1073/pnas.1417614112;
RA Jones S.R., Wilson T.D., Brown M.E., Rahn-Lee L., Yu Y., Fredriksen L.L.,
RA Ozyamak E., Komeili A., Chang M.C.;
RT "Genetic and biochemical investigations of the role of MamP in redox
RT control of iron biomineralization in Magnetospirillum magneticum.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3904-3909(2015).
CC -!- FUNCTION: May play a role in magnetite crystal maturation (Probable).
CC May transfer electrons to balance the Fe(2+)-Fe(3+) ratio during
CC magnetite formation (Probable). {ECO:0000305|PubMed:20212111,
CC ECO:0000305|PubMed:23176475}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000305|PubMed:23176475};
CC Note=Probably binds 2 heme groups via the 2 magnetochrome (MCR) motifs.
CC {ECO:0000305|PubMed:23176475};
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Part of the probable 18 gene mamAB operon.
CC {ECO:0000305|PubMed:20212111}.
CC -!- DISRUPTION PHENOTYPE: Cells have a weak magnetic response and make
CC magnetosome membranes. Magnetosomes are about half the size of wild-
CC type, but nearly as numerous (PubMed:20212111). Deletion of this gene
CC with amb1002 to amb1007 give smaller, elongated magnetite crystals,
CC does not alter subcellular localization of MamC, MamF, MamI or MmsF
CC (PubMed:25775527). 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:25775527}.
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 MamT family. {ECO:0000305}.
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DR EMBL; AP007255; BAE49780.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2W8P5; -.
DR EnsemblBacteria; BAE49780; BAE49780; amb0976.
DR KEGG; mag:amb0976; -.
DR HOGENOM; CLU_1523388_0_0_5; -.
DR OMA; IKCHDIV; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110146; C:magnetosome membrane; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR040963; MCR.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF18509; MCR; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Heme; Iron; Magnetosome; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..176
FT /note="Magnetosome protein MamT"
FT /id="PRO_0000447786"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..176
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 89..109
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:23176475"
FT MOTIF 140..160
FT /note="MCR 2"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 106
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 154
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 157
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 158
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:23176475"
FT MUTAGEN 103..107
FT /note="CIQCH->AIQAA: Loss of magnetic response, no
FT restoration of magnetite particle size."
FT /evidence="ECO:0000269|PubMed:25775527"
FT MUTAGEN 154..158
FT /note="CIKCH->AIKAA: Loss of magnetic response, no
FT restoration of magnetite particle size."
FT /evidence="ECO:0000269|PubMed:25775527"
SQ SEQUENCE 176 AA; 19255 MW; D8F7D98D80BA49C1 CRC64;
MSMEAPRRGR RWVSLGMIAL LAAIGLGLYW DQLSTPSGIT PATSPRRAEG LLLGRLPLPM
EPSLLSPLER LLEPPLRYKL MTIRHIPPVK PGTGMPHPYV GDCIQCHLMV GGPAAGSQFK
TPYGAVLENL SRVRKLGPPI LPTSRQPHPP AGRCIKCHDI VVKVPVDKKG GMRWQL
