MAMA_MAGGM
ID MAMA_MAGGM Reviewed; 217 AA.
AC Q93DY9; V6F5J2;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Magnetosome protein MamA {ECO:0000305};
DE AltName: Full=MM24.3 {ECO:0000303|PubMed:11571158};
GN Name=mamA {ECO:0000303|PubMed:11571158}; OrderedLocusNames=MGMSRv2__2371;
GN ORFNames=mgI495, MGR_4099;
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-23, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=11571158; DOI=10.1128/aem.67.10.4573-4582.2001;
RA Grunberg K., Wawer C., Tebo B.M., Schuler D.;
RT "A large gene cluster encoding several magnetosome proteins is conserved in
RT different species of magnetotactic bacteria.";
RL Appl. Environ. Microbiol. 67:4573-4582(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE OPERON, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=13129949; DOI=10.1128/jb.185.19.5779-5790.2003;
RA Schuebbe S., Kube M., Scheffel A., Wawer C., Heyen U., Meyerdierks A.,
RA Madkour M.H., Mayer F., Reinhardt R., Schueler D.;
RT "Characterization of a spontaneous nonmagnetic mutant of Magnetospirillum
RT gryphiswaldense reveals a large deletion comprising a putative magnetosome
RT island.";
RL J. Bacteriol. 185:5779-5790(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=16237001; DOI=10.1128/jb.187.21.7176-7184.2005;
RA Ullrich S., Kube M., Schuebbe S., Reinhardt R., Schueler D.;
RT "A hypervariable 130-kilobase genomic region of Magnetospirillum
RT gryphiswaldense comprises a magnetosome island which undergoes frequent
RT rearrangements during stationary growth.";
RL J. Bacteriol. 187:7176-7184(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=17449609; DOI=10.1128/jb.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24625872; DOI=10.1128/genomea.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:0-0(2014).
RN [6]
RP PROTEIN SEQUENCE OF 1-12, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=14766587; DOI=10.1128/aem.70.2.1040-1050.2004;
RA Gruenberg K., Mueller E.C., Otto A., Reszka R., Linder D., Kube M.,
RA Reinhardt R., Schueler D.;
RT "Biochemical and proteomic analysis of the magnetosome membrane in
RT Magnetospirillum gryphiswaldense.";
RL Appl. Environ. Microbiol. 70:1040-1050(2004).
RN [7]
RP MINIMAL MAGNETOSOME ISLAND.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=22043287; DOI=10.1371/journal.pone.0025561;
RA Lohsse A., Ullrich S., Katzmann E., Borg S., Wanner G., Richter M.,
RA Voigt B., Schweder T., Schueler D.;
RT "Functional analysis of the magnetosome island in Magnetospirillum
RT gryphiswaldense: the mamAB operon is sufficient for magnetite
RT biomineralization.";
RL PLoS ONE 6:E25561-E25561(2011).
RN [8]
RP PROBABLE SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24816605; DOI=10.1128/jb.01716-14;
RA Lohsse A., Borg S., Raschdorf O., Kolinko I., Tompa E., Posfai M.,
RA Faivre D., Baumgartner J., Schueler D.;
RT "Genetic dissection of the mamAB and mms6 operons reveals a gene set
RT essential for magnetosome biogenesis in Magnetospirillum gryphiswaldense.";
RL J. Bacteriol. 196:2658-2669(2014).
RN [9] {ECO:0007744|PDB:3AS8, ECO:0007744|PDB:3ASF}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 41-217, POSSIBLE FUNCTION,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF 1-MET--ASN-41 AND 1-MET--LEU-26.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
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. Required for formation of functional
CC magnetosomes from pre-existing vesicles. {ECO:0000305|PubMed:21784982}.
CC -!- SUBUNIT: Forms round, 20 nm diameter complexes with a central cavity
CC (PubMed:21784982). Probably binds MamC (Probable). Interacts with full-
CC length Mms6 (By similarity). {ECO:0000250|UniProtKB:Q2W8Q0,
CC ECO:0000269|PubMed:21784982, ECO:0000305|PubMed:24816605}.
CC -!- INTERACTION:
CC Q93DY9; Q93DY9: mamA; NbExp=2; IntAct=EBI-15937405, EBI-15937405;
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}; Peripheral
CC membrane protein {ECO:0000305|PubMed:14766587}. Note=Purified
CC magnetosomes remain attached to each other (PubMed:11571158). Probably
CC a peripheral membrane protein, it is solubilized by Tween 20
CC (PubMed:14766587). Forms oligomers that cover the surface of the
CC magnetosome (By similarity). {ECO:0000250|UniProtKB:Q2W8Q0,
CC ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
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: Normal magnetic response, many fewer
CC magnetosomes. MamC is mislocalized in punctate spots throughout the
CC cell (PubMed:24816605). Deletion of approximately 80 kb of DNA,
CC including this operon, leads to cells that are non-magnetic, lack
CC internal membrane systems, grow poorly, have reduced mobility and take-
CC up and accumulate iron poorly (PubMed:13129949).
CC {ECO:0000269|PubMed:13129949, ECO:0000269|PubMed:24816605}.
CC -!- MISCELLANEOUS: The second most abundant protein in purified
CC magnetosomes. {ECO:0000269|PubMed:11571158}.
CC -!- MISCELLANEOUS: This bacteria makes up to 60 cubo-octahedral
CC magnetosomes of about 45 nm in diameter which contain membrane-bound
CC crystals of magnetite (Fe(3)O(4)). {ECO:0000305|PubMed:11571158}.
CC -!- MISCELLANEOUS: Expression of just the minimal mamAB gene cluster
CC (MGMSRv2__2365 to MGMSRv2__2381), including this gene, is sufficient to
CC form a minimal magnetosome chain with small magnetite particles.
CC {ECO:0000269|PubMed:22043287}.
CC -!- SIMILARITY: Belongs to the magnetosome MamA family. {ECO:0000305}.
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DR EMBL; AF374354; AAL09996.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12040.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30124.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78031.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99586.1; -; Genomic_DNA.
DR PDB; 3AS8; X-ray; 2.00 A; A=41-217.
DR PDB; 3ASF; X-ray; 2.39 A; A/B=41-217.
DR PDBsum; 3AS8; -.
DR PDBsum; 3ASF; -.
DR AlphaFoldDB; Q93DY9; -.
DR SMR; Q93DY9; -.
DR DIP; DIP-60389N; -.
DR STRING; 1430440.MGMSRv2_2371; -.
DR EnsemblBacteria; CDK99586; CDK99586; MGMSRv2__2371.
DR KEGG; mgry:MSR1_03440; -.
DR KEGG; mgy:MGMSRv2__2371; -.
DR eggNOG; COG0457; Bacteria.
DR HOGENOM; CLU_1271021_0_0_5; -.
DR EvolutionaryTrace; Q93DY9; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0110143; C:magnetosome; IDA:UniProtKB.
DR GO; GO:0110146; C:magnetosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 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; Direct protein sequencing; Magnetosome;
KW Membrane; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..217
FT /note="Magnetosome protein MamA"
FT /id="PRO_0000447732"
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"
FT /evidence="ECO:0000305|PubMed:21784982"
FT REGION 113..217
FT /note="C-terminal domain"
FT /evidence="ECO:0000305|PubMed:21784982"
FT MUTAGEN 1..41
FT /note="Missing: No longer forms homooligomeric complexes."
FT /evidence="ECO:0000269|PubMed:21784982"
FT MUTAGEN 1..26
FT /note="Missing: Forms asymmetric and broken homooligomeric
FT complexes."
FT /evidence="ECO:0000269|PubMed:21784982"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3AS8"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3AS8"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:3AS8"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:3AS8"
SQ SEQUENCE 217 AA; 24012 MW; E519659A3D3A8632 CRC64;
MSSKPSNMLD EVTLYTHYGL SVAKKLGANM VDAFRSAFSV NDDIRQVYYR DKGISHAKAG
RYSEAVVMLE QVYDADAFDV EVALHLGIAY VKTGAVDRGT ELLERSIADA PDNIKVATVL
GLTYVQVQKY DLAVPLLVKV AEANPVNFNV RFRLGVALDN LGRFDEAIDS FKIALGLRPN
EGKVHRAIAY SYEQMGSHEE ALPHFKKANE LDERSAV
