MAMF_MAGGM
ID MAMF_MAGGM Reviewed; 111 AA.
AC Q6NE74; V6F254;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Magnetosome protein MamF {ECO:0000305};
GN Name=mamF {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2395;
GN ORFNames=mgI464, MGR_4076;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
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 [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-12, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND PROTEOLYTIC CLEAVAGE.
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 [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=18539817; DOI=10.1128/aem.00231-08;
RA Lang C., Schueler D.;
RT "Expression of green fluorescent protein fused to magnetosome proteins in
RT microaerophilic magnetotactic bacteria.";
RL Appl. Environ. Microbiol. 74:4944-4953(2008).
RN [7]
RP FUNCTION, PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=17965152; DOI=10.1128/jb.01371-07;
RA Scheffel A., Gaerdes A., Gruenberg K., Wanner G., Schueler D.;
RT "The major magnetosome proteins MamGFDC are not essential for magnetite
RT biomineralization in Magnetospirillum gryphiswaldense but regulate the size
RT of magnetosome crystals.";
RL J. Bacteriol. 190:377-386(2008).
RN [8]
RP FUNCTION, 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).
CC -!- FUNCTION: Plays a role in regulating magnetite crystal size; partially
CC redundant function with MmsF. {ECO:0000269|PubMed:17965152,
CC ECO:0000269|PubMed:24816605}.
CC -!- SUBUNIT: May form homooligomers. {ECO:0000305|PubMed:14766587}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:14766587, ECO:0000269|PubMed:18539817}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Resistant to trypsin digestion in
CC isolated magnetosomes (PubMed:14766587). Localizes as a filament-like
CC structure in a straight line running through the center of the cell, in
CC a position that corresponds to magnetosomes (PubMed:18539817). Requires
CC MamE for correct localization (By similarity).
CC {ECO:0000250|UniProtKB:Q2W8R8, ECO:0000269|PubMed:14766587,
CC ECO:0000269|PubMed:18539817}.
CC -!- INDUCTION: Part of the probable 4 gene mamGFDC operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- PTM: Subject to cleavage or degradation; identified by N-terminal
CC sequencing of proteins that are about 103, 92 and 15 kDa in size.
CC {ECO:0000269|PubMed:14766587}.
CC -!- DISRUPTION PHENOTYPE: Normal magnetic response, no change in
CC magnetosome size or number. A double mamF-mmsF deletion has a normal
CC magnetic response, slightly smaller, fewer magnetosomes
CC (PubMed:24816605). Deletion of any 2 genes encoded in this operon
CC (mamC, mamD, mamF and mamG) decreases crystal size regardless of the
CC protein combination. Deletion of the mamGFDC operon leads to smaller
CC magnetite crystals in irregularly spaced chains, but no other phenotype
CC (PubMed:17965152). Deletion of approximately 80 kb of DNA, including
CC this operon, leads to cells that are non-magnetic, lack internal
CC membrane systems, grow poorly, have reduced mobility and take-up and
CC accumulate iron poorly (PubMed:13129949). {ECO:0000269|PubMed:13129949,
CC ECO:0000269|PubMed:17965152, ECO:0000269|PubMed:24816605}.
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:13129949}.
CC -!- SIMILARITY: Belongs to the magnetosome MamF/MmsF protein family.
CC {ECO:0000305|PubMed:24816605}.
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DR EMBL; BX571797; CAE12019.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30100.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78008.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99610.1; -; Genomic_DNA.
DR RefSeq; WP_024080604.1; NZ_CP027526.1.
DR AlphaFoldDB; Q6NE74; -.
DR STRING; 1430440.MGMSRv2_2395; -.
DR TCDB; 9.B.89.1.1; the putative channel-forming 3 tmss mamf (mamf) family.
DR EnsemblBacteria; CDK99610; CDK99610; MGMSRv2__2395.
DR KEGG; mgry:MSR1_03200; -.
DR KEGG; mgy:MGMSRv2__2395; -.
DR eggNOG; COG4818; Bacteria.
DR HOGENOM; CLU_095018_0_1_5; -.
DR OrthoDB; 1774376at2; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110146; C:magnetosome membrane; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Biomineralization; Direct protein sequencing; Magnetosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..111
FT /note="Magnetosome protein MamF"
FT /id="PRO_0000447795"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..50
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..111
FT /note="Lumenal"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12336 MW; B31A034FD6970C51 CRC64;
MAETILIETK TAGGNCRSYL MAGASYLGIL CFVPLLMSRD DEYVYFHAKQ GLVLWMWSIL
AMFALHLPGI GKWLFGFSSM GVLMLSVVGL VSVALRRTWR LPLISHVVAL I
