MAMA_MAGSA
ID MAMA_MAGSA Reviewed; 217 AA.
AC Q2W8Q0; Q50224;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Magnetosome protein MamA {ECO:0000305};
GN Name=mamA {ECO:0000303|PubMed:15004275};
GN Synonyms=mms24 {ECO:0000303|PubMed:16303747}; OrderedLocusNames=amb0971;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=15004275; DOI=10.1073/pnas.0400391101;
RA Komeili A., Vali H., Beveridge T.J., Newman D.K.;
RT "Magnetosome vesicles are present before magnetite formation, and MamA is
RT required for their activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3839-3844(2004).
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, 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 [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20439702; DOI=10.1073/pnas.1001870107;
RA Yamamoto D., Taoka A., Uchihashi T., Sasaki H., Watanabe H., Ando T.,
RA Fukumori Y.;
RT "Visualization and structural analysis of the bacterial magnetic organelle
RT magnetosome using atomic force microscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9382-9387(2010).
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 INDUCTION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=25048532; DOI=10.1111/1574-6968.12541;
RA Taoka A., Eguchi Y., Mise S., Oestreicher Z., Uno F., Fukumori Y.;
RT "A magnetosome-associated cytochrome MamP is critical for magnetite crystal
RT growth during the exponential growth phase.";
RL FEMS Microbiol. Lett. 358:21-29(2014).
RN [7]
RP INTERACTION WITH MMS6, AND SUBCELLULAR LOCATION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=28955887; DOI=10.1016/j.bbrep.2016.05.010;
RA Nguyen H.V., Suzuki E., Oestreicher Z., Minamide H., Endoh H., Fukumori Y.,
RA Taoka A.;
RT "A protein-protein interaction in magnetosomes: TPR protein MamA interacts
RT with an Mms6 protein.";
RL Biochem. Biophys. Rep. 7:39-44(2016).
RN [8] {ECO:0007744|PDB:3AS4, ECO:0007744|PDB:3AS5, ECO:0007744|PDB:3ASD, ECO:0007744|PDB:3ASG, ECO:0007744|PDB:3ASH}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 37-213, POSSIBLE FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 1-MET--ASN-41;
RP 1-MET--LEU-26 AND ARG-50.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=21784982; DOI=10.1073/pnas.1103367108;
RA Zeytuni N., Ozyamak E., Ben-Harush K., Davidov G., Levin M., Gat Y.,
RA Moyal T., Brik A., Komeili A., Zarivach R.;
RT "Self-recognition mechanism of MamA, a magnetosome-associated TPR-
RT containing protein, promotes complex assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E480-E487(2011).
CC -!- FUNCTION: Probably forms a large homooligomer on which other
CC magnetosome subunits assemble (Probable). Required for formation of
CC functional magnetosomes from pre-existing vesicles, it has a dynamic
CC location in the cell (PubMed:15004275). {ECO:0000269|PubMed:15004275,
CC ECO:0000305|PubMed:21784982}.
CC -!- SUBUNIT: Oligomerizes into high molecular weight complexes (at least
CC 560 kDa) (PubMed:28955887, PubMed:20439702). Forms round, 20 nm
CC diameter complexes with a central cavity (PubMed:21784982). Interacts
CC with full-length Mms6 (PubMed:28955887). Probably binds MamC (By
CC similarity). {ECO:0000250|UniProtKB:Q93DY9,
CC ECO:0000269|PubMed:20439702, ECO:0000269|PubMed:21784982,
CC ECO:0000269|PubMed:28955887}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:15004275, ECO:0000269|PubMed:16303747,
CC ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:20439702,
CC ECO:0000269|PubMed:21784982, ECO:0000269|PubMed:28955887}; Peripheral
CC membrane protein {ECO:0000269|PubMed:20439702,
CC ECO:0000269|PubMed:28955887}. Note=Reversibly binds to magnetosomes
CC (PubMed:20439702). Forms oligomers that cover the surface of the
CC magnetosome (PubMed:20439702). Its location is dynamic; in log phase
CC cells tagged protein extends from one pole to the other, which is
CC longer than the magnetosome chain and is occasionally associated with
CC the inner membrane. In stationary phase it forms 3-4 spots in the cell
CC (PubMed:15004275, PubMed:21784982). {ECO:0000269|PubMed:15004275,
CC ECO:0000269|PubMed:20439702, ECO:0000269|PubMed:21784982}.
CC -!- INDUCTION: Constitutively expressed, levels remain the same over 144
CC hours of growth (at protein level) (PubMed:25048532). Part of the
CC probable 18 gene mamAB operon (Probable). {ECO:0000269|PubMed:25048532,
CC ECO:0000305|PubMed:20212111}.
CC -!- DOMAIN: Protein missing TPR1 (residues 1-41) forms an N-terminal domain
CC of TPR 2-3 and a C-terminal domain with TPR 4-6 which can move with
CC respect to each other, hinged at D-112. {ECO:0000269|PubMed:21784982}.
CC -!- DISRUPTION PHENOTYPE: Takes up less Fe(3+) than wild-type cells, is
CC less responsive to magnetic field, cells have 1-5 magnetosomes
CC (compared to 8-14 in wild-type). Cells have chains of empty vesicles
CC (PubMed:15004275). Magnetosomes are slightly further apart than in
CC wild-type (PubMed:20439702). Deletion of genes mamH to mamV (amb0961 to
CC amb0978) gives cells with no magnetosomes and no magnetic response
CC (PubMed:20212111). {ECO:0000269|PubMed:15004275,
CC ECO:0000269|PubMed:20212111, ECO:0000269|PubMed:20439702}.
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 MamA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE49775.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY508230; AAR90856.1; -; Genomic_DNA.
DR EMBL; AP007255; BAE49775.1; ALT_INIT; Genomic_DNA.
DR PDB; 3AS4; X-ray; 2.33 A; A=37-213.
DR PDB; 3AS5; X-ray; 2.00 A; A/B=37-213.
DR PDB; 3ASD; X-ray; 2.45 A; A=37-213.
DR PDB; 3ASG; X-ray; 2.33 A; A/B=37-213.
DR PDB; 3ASH; X-ray; 2.41 A; A/B=37-213.
DR PDBsum; 3AS4; -.
DR PDBsum; 3AS5; -.
DR PDBsum; 3ASD; -.
DR PDBsum; 3ASG; -.
DR PDBsum; 3ASH; -.
DR AlphaFoldDB; Q2W8Q0; -.
DR SMR; Q2W8Q0; -.
DR STRING; 342108.amb0971; -.
DR EnsemblBacteria; BAE49775; BAE49775; amb0971.
DR KEGG; mag:amb0971; -.
DR HOGENOM; CLU_1271021_0_0_5; -.
DR OrthoDB; 1047663at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0110143; C:magnetosome; IDA:UniProtKB.
DR GO; GO:0110146; C:magnetosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0110148; P:biomineralization; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF07719; TPR_2; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biomineralization; Magnetosome; Membrane; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..217
FT /note="Magnetosome protein MamA"
FT /id="PRO_0000447733"
FT REPEAT 12..44
FT /note="TPR 1"
FT /evidence="ECO:0000305|PubMed:21784982"
FT REPEAT 46..79
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 80..113
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 114..147
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 148..181
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 182..215
FT /note="TPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REGION 41..112
FT /note="N-terminal domain (NTD)"
FT /evidence="ECO:0000305|PubMed:21784982"
FT REGION 113..217
FT /note="C-terminal domain (CTD)"
FT /evidence="ECO:0000305|PubMed:21784982"
FT SITE 50
FT /note="Salt bridge that stabilizes NTD"
FT /evidence="ECO:0000305|PubMed:21784982"
FT SITE 79
FT /note="Salt bridge that stabilizes NTD"
FT /evidence="ECO:0000305|PubMed:21784982"
FT MUTAGEN 1..41
FT /note="Missing: No longer forms homooligomeric complexes,
FT no longer associates with magnetosomes."
FT /evidence="ECO:0000269|PubMed:21784982"
FT MUTAGEN 1..26
FT /note="Missing: No longer associates with magnetosomes,
FT protein is unstable."
FT /evidence="ECO:0000269|PubMed:21784982"
FT MUTAGEN 50
FT /note="R->E: Protein no longer associates with
FT magnetosomes, no longer forms homooligomeric complexes, a
FT crystal of 41-217 has a large rotation of the NTD."
FT /evidence="ECO:0000269|PubMed:21784982"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3AS5"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3AS5"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3ASG"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:3AS5"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:3AS5"
SQ SEQUENCE 217 AA; 23976 MW; C90477FE83E6B483 CRC64;
MSSKPSDILD EVTLYAHYGL SVAKKLGMNM VDAFRAAFSV NDDIRQVYYR DKGISHAKAG
RYSQAVMLLE QVYDADAFDV DVALHLGIAY VKTGAVDRGT ELLERSLADA PDNVKVATVL
GLTYVQVQKY DLAVPLLIKV AEANPINFNV RFRLGVALDN LGRFDEAIDS FKIALGLRPN
EGKVHRAIAF SYEQMGRHEE ALPHFKKANE LDEGASV
