MAMD_MAGGM
ID MAMD_MAGGM Reviewed; 314 AA.
AC Q93DY2; Q6NE73; V6F2D1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Magnetosome protein MamD {ECO:0000305};
DE AltName: Full=MM21.9 {ECO:0000303|PubMed:11571158};
GN Name=mamD {ECO:0000303|PubMed:11571158}; OrderedLocusNames=MGMSRv2__2394;
GN ORFNames=mgI466, MGR_4077;
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 1-6, AND SUBCELLULAR
RP 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 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 SUBCELLULAR LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=29243866; DOI=10.1111/mmi.13899;
RA Uebe R., Keren-Khadmy N., Zeytuni N., Katzmann E., Navon Y., Davidov G.,
RA Bitton R., Plitzko J.M., Schuler D., Zarivach R.;
RT "The dual role of MamB in magnetosome membrane assembly and magnetite
RT biomineralization.";
RL Mol. Microbiol. 107:542-557(2018).
CC -!- FUNCTION: Helps regulate magnetite crystal morphology, probably in a
CC single growth axis (By similarity). Plays a role in regulating
CC magnetite crystal size (PubMed:17965152). Probably binds Fe(2+) (By
CC similarity). {ECO:0000250|UniProtKB:Q2W8R9,
CC ECO:0000269|PubMed:17965152}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587,
CC ECO:0000269|PubMed:29243866}; Single-pass membrane protein
CC {ECO:0000255}. Note=Purified magnetosomes remain attached to each
CC other. {ECO:0000269|PubMed:11571158}.
CC -!- INDUCTION: Part of the probable 4 gene mamGFDC operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- DOMAIN: The isolated charged lumenal magnetite-interacting component
CC (MIC, residues 298-314) binds Fe(2+). {ECO:0000250|UniProtKB:Q2W8R9}.
CC -!- PTM: Seen in gels as a band of about 7 kDa, suggesting it may undergo
CC cleavage. {ECO:0000250|UniProtKB:Q2W8R9}.
CC -!- DISRUPTION PHENOTYPE: 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}.
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 -!- SIMILARITY: Belongs to the magnetosome MamD/Mms5 family. {ECO:0000305}.
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DR EMBL; AF374355; AAL10003.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12020.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30102.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78009.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99609.1; -; Genomic_DNA.
DR RefSeq; WP_024080603.1; NZ_CP027526.1.
DR AlphaFoldDB; Q93DY2; -.
DR STRING; 1430440.MGMSRv2_2394; -.
DR EnsemblBacteria; CDK99609; CDK99609; MGMSRv2__2394.
DR KEGG; mgry:MSR1_03210; -.
DR KEGG; mgy:MGMSRv2__2394; -.
DR HOGENOM; CLU_815860_0_0_5; -.
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.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Biomineralization; Direct protein sequencing; Iron; Magnetosome; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Magnetosome protein MamD"
FT /id="PRO_0000447792"
FT TOPO_DOM 1..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..314
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 263..270
FT /note="GL repeat"
FT /evidence="ECO:0000305"
FT REGION 298..314
FT /note="Magnetite-interacting component (MIC), binds Fe(2+)"
FT /evidence="ECO:0000250|UniProtKB:Q2W8R9"
FT CONFLICT 227
FT /note="A -> V (in Ref. 1; AAL10003, 2; CAE12020, 3;
FT CAJ30102 and 4; CAM78009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 30227 MW; BF5E7250E3A721CD CRC64;
MQDLFLAKVE SAMQASQVGA LAGQTATVSS VSATTNLATI TPTTAGQAPI IVKLDAARQV
TELQALMGKT VLVGKTPTTI GGIGNWIALT PAAGAKTGAA VAGTGQLVMM KVEGTGAAIK
LPALAGKSFI VAQPPVAAGT KAAGMLYLNP VGGGDMVAIN IQNAMTQTGG LVGKTFTVAP
SPVIGGTTGK FLVLKPMATG VGKAVGSGAV VAKFVPAAVT GTGGAAAIGA GSATTLMATG
ASTITPVTAA AAGSAMLTAK GVGLGLGLGL GAWGPFALGA IGLAGVVALY TWARRRHGAP
DVSDDALLAA VGEE
