MAMC_MAGSA
ID MAMC_MAGSA Reviewed; 124 AA.
AC Q2W8S0; Q83VL9;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Magnetosome protein MamC {ECO:0000305};
GN Name=mamC {ECO:0000303|PubMed:21414040};
GN Synonyms=mms13 {ECO:0000303|PubMed:12496282}; OrderedLocusNames=amb0951;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 2-42, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=12496282; DOI=10.1074/jbc.m211729200;
RA Arakaki A., Webb J., Matsunaga T.;
RT "A novel protein tightly bound to bacterial magnetic particles in
RT Magnetospirillum magneticum strain AMB-1.";
RL J. Biol. Chem. 278:8745-8750(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUBCELLULAR LOCATION.
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 [3]
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 [4]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=22846572; DOI=10.1016/j.bbrc.2012.07.116;
RA Kanetsuki Y., Tanaka M., Tanaka T., Matsunaga T., Yoshino T.;
RT "Effective expression of human proteins on bacterial magnetic particles in
RT an anchor gene deletion mutant of Magnetospirillum magneticum AMB-1.";
RL Biochem. Biophys. Res. Commun. 426:7-11(2012).
RN [5]
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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=24961165; DOI=10.1111/mmi.12683;
RA Arakaki A., Yamagishi A., Fukuyo A., Tanaka M., Matsunaga T.;
RT "Co-ordinated functions of Mms proteins define the surface structure of
RT cubo-octahedral magnetite crystals in magnetotactic bacteria.";
RL Mol. Microbiol. 93:554-567(2014).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27481925; DOI=10.1128/jb.00280-16;
RA Arakaki A., Kikuchi D., Tanaka M., Yamagishi A., Yoda T., Matsunaga T.;
RT "Comparative subcellular localization analysis of magnetosome proteins
RT reveals a unique localization behavior of Mms6 protein onto magnetite
RT crystals.";
RL J. Bacteriol. 198:2794-2802(2016).
RN [8]
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).
RN [9]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-49.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=30405554; DOI=10.3389/fmicb.2018.02480;
RA Nudelman H., Lee Y.Z., Hung Y.L., Kolusheva S., Upcher A., Chen Y.C.,
RA Chen J.Y., Sue S.C., Zarivach R.;
RT "Understanding the biomineralization role of magnetite-interacting
RT components (MICs) from magnetotactic bacteria.";
RL Front. Microbiol. 9:2480-2480(2018).
RN [10] {ECO:0007744|PDB:5E7U, ECO:0007744|PDB:5I69}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 36-56, FUNCTION, DOMAIN,
RP IRON-BINDING, TOPOLOGY, AND MUTAGENESIS OF 45-GLU--ASP-49; GLU-45 AND
RP ASP-49.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=26970040; DOI=10.1016/j.jsb.2016.03.001;
RA Nudelman H., Tercedor C.V., Kolusheva S., Gonzalez T.P., Widdrat M.,
RA Grimberg N., Levi H., Nelkenbaum O., Davidov G., Faivre D.,
RA Jimenez-Lopez C., Zarivach R.;
RT "Structure-function studies of the magnetite-biomineralizing magnetosome-
RT associated protein MamC.";
RL J. Struct. Biol. 194:244-252(2016).
RN [11] {ECO:0007744|PDB:5MM3, ECO:0007744|PDB:6EQZ}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 36-56, AND DOMAIN.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=29372895; DOI=10.1107/s2059798317017491;
RA Nudelman H., Gonzalez T.P., Kolushiva S., Widdrat M., Reichel V.,
RA Davidov G., Bitton R., Faivre D., Lopez C.J., Zarivach R.;
RT "The importance of the helical structure of a MamC-derived magnetite-
RT interacting peptide for its function in magnetite formation.";
RL Acta Crystallogr. D 74:10-20(2018).
CC -!- FUNCTION: Probably involved in magnetite crystal growth (Probable). The
CC lumenal domain may bind the magnetite crystals, affecting crystal size
CC and shape (Probable). {ECO:0000305|PubMed:24961165,
CC ECO:0000305|PubMed:26970040, ECO:0000305|PubMed:30405554}.
CC -!- SUBUNIT: Probably interacts with MamA. {ECO:0000250|UniProtKB:Q93DY1}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:12496282, ECO:0000269|PubMed:16303747,
CC ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:27481925,
CC ECO:0000269|PubMed:28790202, ECO:0000305|PubMed:22846572}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Tightly associated with magnetite
CC crystals (PubMed:12496282). Tagged protein forms straight lines with a
CC punctate pattern extending along most of the cell associated with its
CC inner curvature, in the correct position to be associated with
CC magnetite-containing magnetosomes (PubMed:21414040, PubMed:27481925,
CC PubMed:28790202). In a mamE disruption MamC forms 1-2 foci in the cell
CC (PubMed:21414040). {ECO:0000269|PubMed:12496282,
CC ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:27481925,
CC ECO:0000269|PubMed:28790202}.
CC -!- DOMAIN: The lumenal magnetite interacting component (MIC, residues 36-
CC 56) binds magnetite in vitro when fused C-terminally to maltose-binding
CC protein (PubMed:26970040). Isolated MIC binds poorly to Fe(2+), Fe(3+),
CC or Ni(2+), but improves quality of iron particles during iron co-
CC precipitation experiments (PubMed:30405554). The lumenal loop (MIC)
CC probably has to form a helix to interact with magnetite
CC (PubMed:29372895). {ECO:0000269|PubMed:26970040,
CC ECO:0000269|PubMed:29372895, ECO:0000269|PubMed:30405554}.
CC -!- DISRUPTION PHENOTYPE: No growth phenotype, magnetite crystals are
CC slightly smaller with a wild-type surface (PubMed:22846572,
CC PubMed:24961165). Deletion of the probable mamGFDC operon leads to a
CC slight reduction in magnetic response and slightly narrower magnetite
CC crystals (PubMed:22716969). {ECO:0000269|PubMed:22716969,
CC ECO:0000269|PubMed:22846572, ECO:0000269|PubMed:24961165}.
CC -!- BIOTECHNOLOGY: Foreign proteins fused to the N-terminal membrane-
CC targeted domain of this protein are expressed on the magnetosome
CC membrane, subsequent purification of the fusion protein occurs by
CC extracting the organelles from the lysed bacteria using magnets. In
CC this study human thyroid-stimulating hormone receptor (TSHR) and class
CC II major histocompatibility complex (MHC II) were expressed and
CC purified; expression is better when the endogenous gene is deleted.
CC {ECO:0000269|PubMed:22846572}.
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 MamC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE49755.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB096081; BAC65160.1; -; Genomic_DNA.
DR EMBL; AP007255; BAE49755.1; ALT_INIT; Genomic_DNA.
DR PDB; 5E7U; X-ray; 2.80 A; A=36-57.
DR PDB; 5I69; X-ray; 2.70 A; A=36-57.
DR PDB; 5MM3; X-ray; 2.10 A; A/B=57-78.
DR PDB; 6EQZ; X-ray; 2.29 A; A/B/D/G=36-56.
DR PDBsum; 5E7U; -.
DR PDBsum; 5I69; -.
DR PDBsum; 5MM3; -.
DR PDBsum; 6EQZ; -.
DR AlphaFoldDB; Q2W8S0; -.
DR SMR; Q2W8S0; -.
DR TCDB; 9.B.90.1.2; the putative channel forming 2 tmss mamc (mamc) family.
DR EnsemblBacteria; BAE49755; BAE49755; amb0951.
DR KEGG; mag:amb0951; -.
DR HOGENOM; CLU_1989955_0_0_5; -.
DR OrthoDB; 1848743at2; -.
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 3D-structure; Biomineralization; Direct protein sequencing; Iron;
KW Magnetosome; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12496282"
FT CHAIN 2..124
FT /note="Magnetosome protein MamC"
FT /id="PRO_0000447790"
FT TOPO_DOM 2..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..64
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26970040"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 36..56
FT /note="MIC, when fused with the C-terminus of maltose-
FT binding protein (MBP) or expressed as a fragment, improves
FT quality of iron particles during precipitation experiments,
FT binds magnetite"
FT /evidence="ECO:0000269|PubMed:26970040,
FT ECO:0000269|PubMed:30405554"
FT MUTAGEN 45..49
FT /note="EAAID->AAAIA: Fused MIC no longer improves iron
FT particles, does not bind magnetite."
FT /evidence="ECO:0000269|PubMed:26970040"
FT MUTAGEN 45
FT /note="E->A: Fused MIC no longer improves iron particles,
FT does not bind magnetite."
FT /evidence="ECO:0000269|PubMed:26970040"
FT MUTAGEN 49
FT /note="D->A: MIC expressed as a fragment or fused to MBP no
FT longer improves iron particles, binds magnetite."
FT /evidence="ECO:0000269|PubMed:26970040,
FT ECO:0000269|PubMed:30405554"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6EQZ"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6EQZ"
SQ SEQUENCE 124 AA; 12378 MW; BF74752AACA5462B CRC64;
MPFHLAPYLA KSVPGVGVLG ALVGGAAALA KNVRLLKEKR ITNTEAAIDT GKETVGAGLA
TALSAVAATA VGGGLVVSLG TALVAGVAAK YAWDRGVDLV EKELNRGKAA NGASDEDILR
DELA
