MAMC_MAGGM
ID MAMC_MAGGM Reviewed; 125 AA.
AC Q93DY1; Q6NE72; V6F534;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Magnetosome protein MamC {ECO:0000303|PubMed:11571158};
DE AltName: Full=MM15.5 {ECO:0000303|PubMed:11571158};
GN Name=mamC {ECO:0000303|PubMed:11571158}; OrderedLocusNames=MGMSRv2__2393;
GN ORFNames=mgI467, MGR_4078;
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 2-33; 94-113 AND
RP 118-125, AND 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 1-11, 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 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 [8]
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 [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=22007638; DOI=10.1111/j.1365-2958.2011.07863.x;
RA Uebe R., Junge K., Henn V., Poxleitner G., Katzmann E., Plitzko J.M.,
RA Zarivach R., Kasama T., Wanner G., Posfai M., Boettger L., Matzanke B.,
RA Schueler D.;
RT "The cation diffusion facilitator proteins MamB and MamM of
RT Magnetospirillum gryphiswaldense have distinct and complex functions, and
RT are involved in magnetite biomineralization and magnetosome membrane
RT assembly.";
RL Mol. Microbiol. 82:818-835(2011).
RN [10]
RP PROBABLE SUBUNIT.
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
CC (PubMed:17965152). The lumenal domain may bind the magnetite crystals,
CC affecting crystal size and shape (By similarity).
CC {ECO:0000250|UniProtKB:Q2W8S0, ECO:0000269|PubMed:17965152}.
CC -!- SUBUNIT: Probably interacts with MamA. {ECO:0000305|PubMed:24816605}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587,
CC ECO:0000269|PubMed:18539817, ECO:0000269|PubMed:22007638}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Purified magnetosomes remain
CC attached to each other (PubMed:11571158). Resistant to trypsin
CC digestion in isolated magnetosomes (PubMed:14766587). Localizes as a
CC filament-like structure in a straight line running through the center
CC of the cell, in a position that corresponds to magnetosomes
CC (PubMed:18539817, PubMed:22007638). {ECO:0000269|PubMed:11571158,
CC ECO:0000269|PubMed:14766587, ECO:0000269|PubMed:18539817,
CC ECO:0000269|PubMed:22007638}.
CC -!- INDUCTION: Part of the probable 4 gene mamGFDC operon.
CC {ECO:0000305|PubMed:13129949, ECO:0000305|PubMed:17965152}.
CC -!- DOMAIN: The lumenal magnetite interacting component (MIC, residues 36-
CC 56) probably binds magnetite. {ECO:0000250|UniProtKB:Q2W8S0}.
CC -!- DISRUPTION PHENOTYPE: Single gene deletion leads to slightly smaller
CC magnetite crystals, but no other measurable phenotype
CC (PubMed:17965152). 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 operon leads to smaller magnetite
CC 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: The most abundant protein in purified magnetosomes.
CC {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587,
CC ECO:0000305|PubMed:18539817}.
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 MamC family. {ECO:0000305}.
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DR EMBL; AF374355; AAL10004.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12021.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30103.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78010.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99608.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93DY1; -.
DR STRING; 1430440.MGMSRv2_2393; -.
DR TCDB; 9.B.90.1.1; the putative channel forming 2 tmss mamc (mamc) family.
DR EnsemblBacteria; CDK99608; CDK99608; MGMSRv2__2393.
DR KEGG; mgy:MGMSRv2__2393; -.
DR eggNOG; ENOG5033G8Q; Bacteria.
DR HOGENOM; CLU_1989955_0_0_5; -.
DR OrthoDB; 1848743at2; -.
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..125
FT /note="Magnetosome protein MamC"
FT /id="PRO_0000447789"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..64
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 36..56
FT /note="Magnetite interacting component (MIC) binds
FT magnetite"
FT /evidence="ECO:0000250|UniProtKB:Q2W8S0"
FT CONFLICT 81
FT /note="A -> T (in Ref. 1; AAL10004, 3; CAJ30103 and 4;
FT CAM78010)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..125
FT /note="EELA -> DEA (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 125 AA; 12394 MW; 451E23C9B5DA9107 CRC64;
MSFQLAPYLA KSVPGIGILG GIVGGAAALA KNARLLKDKQ ITGTEAAIDT GKEAAGAGLA
TAFSAVAATA VGGGLVVSLG AALIAGVAAK YAWDLGVDFI EKELRHGKSA EATASDEDIL
REELA
