MMS6_MAGGM
ID MMS6_MAGGM Reviewed; 136 AA.
AC Q6NE76; V6F5K9;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Magnetite biomineralization protein Mms6 {ECO:0000305};
DE AltName: Full=Magnetosome protein Mms6 {ECO:0000305};
GN Name=mms6 {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2396;
GN ORFNames=ORF4;
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], AND DISRUPTION 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 [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 [3]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS 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 [4]
RP PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION, PROBABLE OPERON, 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 [6]
RP INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=30367002; DOI=10.1128/aem.02394-18;
RA Wang Q., Wu S., Li X., Zhang T., Yang J., Wang X., Li F., Li Y., Peng Y.,
RA Li J.;
RT "Work Patterns of MamXY Proteins during Magnetosome Formation in
RT Magnetospirillum gryphiswaldense MSR-1.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
CC -!- FUNCTION: Promotes the formation of magnetite in Fe(2+)-rich
CC conditions, when magnetite is not readily formed. Binds both Fe(2+) and
CC Fe(3+). May help control the production of crystals with a specific
CC morphology (By similarity). May function with MamX, MamY amd MamZ in
CC biomineralization (Probable). The 4 genes of this operon collectively
CC influence magnetosome size and number (PubMed:24816605).
CC {ECO:0000250|UniProtKB:Q2W8R5, ECO:0000269|PubMed:24816605,
CC ECO:0000305|PubMed:30367002}.
CC -!- SUBUNIT: Full length protein oligomerizes and interacts with MamA.
CC {ECO:0000250|UniProtKB:Q2W8R5}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:14766587}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Low levels of protein are associated with magnetosomes as
CC they start to develop, rises to a maximum as the magnetosomes mature
CC and then decreases (at protein level) (PubMed:30367002). Part of the
CC probable mms6 operon (Probable). {ECO:0000269|PubMed:30367002,
CC ECO:0000305|PubMed:22043287, ECO:0000305|PubMed:24816605}.
CC -!- DOMAIN: The C-terminal 21 residues (later called magnetite-interacting
CC component, MIC, residues 112-133) self assemble into multimers up to
CC octamers; this fragment binds Fe(3+) which alters its structure. Also
CC binds Fe(2+). {ECO:0000250|UniProtKB:Q2W8R5}.
CC -!- PTM: May undergo cleavage. {ECO:0000250|UniProtKB:Q2W8R5}.
CC -!- DISRUPTION PHENOTYPE: Normal magnetic response, slightly fewer,
CC slightly smaller magnetosomes. A double mms6-mmsF deletion has an
CC intermediate magnetic response, with slightly smaller and fewer
CC magnetosomes than the single mutation (PubMed:24816605). Deletion of
CC the 4 gene operon (mms6, mmsF, mms36 and mms48) gives an intermediate
CC magnetic response with fewer, smaller magnetosomes in irregular pseudo-
CC chains (PubMed:22043287, PubMed:24816605). Deletion of approximately 80
CC kb of DNA, including this gene, leads to cells that are non-magnetic,
CC lack internal membrane systems, grow poorly, have reduced mobility and
CC take-up and accumulate iron poorly (PubMed:13129949).
CC {ECO:0000269|PubMed:13129949, ECO:0000269|PubMed:22043287,
CC 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 Mms6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDK99611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX571797; CAE12017.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99611.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6NE76; -.
DR STRING; 1430440.MGMSRv2_2396; -.
DR EnsemblBacteria; CDK99611; CDK99611; MGMSRv2__2396.
DR KEGG; mgy:MGMSRv2__2396; -.
DR HOGENOM; CLU_1675763_0_0_5; -.
DR OrthoDB; 2091871at2; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110145; C:magnetosome lumen; IDA:UniProtKB.
DR GO; GO:0110146; C:magnetosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Biomineralization; Iron; Magnetosome; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..136
FT /note="Magnetite biomineralization protein Mms6"
FT /id="PRO_0000447814"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..136
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 86..95
FT /note="GL repeat"
FT /evidence="ECO:0000305"
FT REGION 115..136
FT /note="MIC, self-assembles, binds magnetite, Fe(2+) and
FT Fe(3+)"
FT /evidence="ECO:0000250|UniProtKB:Q2W8R5"
SQ SEQUENCE 136 AA; 12689 MW; FDF6F06662D6DFB3 CRC64;
MGEMEREGAT AKVGAGKVGA GKVGAAKAGA APAAAQGAGT KVVAAQGAGT KVVAAQGAGA
KAAAVGVGKV GAGAKAVGGT IWSGKGLALG LGMGLGAWGP LILGVVGAGA VYAYMKSRDI
EAAQSDEEVE LRDALS
