MAMM_MAGGM
ID MAMM_MAGGM Reviewed; 318 AA.
AC V6F235; Q6NE57;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Magnetosome protein MamM {ECO:0000305};
DE AltName: Full=Probable iron transporter MamM {ECO:0000305};
GN Name=mamM {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2375;
GN ORFNames=mgI491, MGR_4095;
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;
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 [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 1-10, 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 [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 6-CYS--CYS-9; CYS-9; TYR-46; ASP-50; HIS-155; ASP-159;
RP 259-THR--ASN-318; 289-GLU--ASN-318 AND 309-ASP--ASN-318.
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 [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 FUNCTION, MINIMAL VESICLE FORMATION GENES, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=27286560; DOI=10.1371/journal.pgen.1006101;
RA Raschdorf O., Forstner Y., Kolinko I., Uebe R., Plitzko J.M., Schueler D.;
RT "Genetic and Ultrastructural Analysis Reveals the Key Players and Initial
RT Steps of Bacterial Magnetosome Membrane Biogenesis.";
RL PLoS Genet. 12:E1006101-E1006101(2016).
RN [9]
RP SUBUNIT, AND DOMAIN.
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).
RN [10] {ECO:0007744|PDB:3W8G}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 215-318, FUNCTION, PROBABLE
RP IRON-BINDING, SUBUNIT, AND MUTAGENESIS OF VAL-260.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24819161; DOI=10.1371/journal.pone.0097154;
RA Zeytuni N., Uebe R., Maes M., Davidov G., Baram M., Raschdorf O.,
RA Friedler A., Miller Y., Schuler D., Zarivach R.;
RT "Bacterial magnetosome biomineralization--a novel platform to study
RT molecular mechanisms of human CDF-related Type-II diabetes.";
RL PLoS ONE 9:E97154-E97154(2014).
RN [11] {ECO:0007744|PDB:3W5X, ECO:0007744|PDB:3W5Y, ECO:0007744|PDB:3W5Z, ECO:0007744|PDB:3W60, ECO:0007744|PDB:3W61, ECO:0007744|PDB:3W62, ECO:0007744|PDB:3W63, ECO:0007744|PDB:3W64, ECO:0007744|PDB:3W65, ECO:0007744|PDB:3W66, ECO:0007744|PDB:3W8P}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 215-318, FUNCTION, PROBABLE
RP IRON-BINDING, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-249; VAL-260;
RP HIS-264; HIS-285 AND GLU-289.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24658343; DOI=10.1371/journal.pone.0092141;
RA Zeytuni N., Uebe R., Maes M., Davidov G., Baram M., Raschdorf O.,
RA Nadav-Tsubery M., Kolusheva S., Bitton R., Goobes G., Friedler A.,
RA Miller Y., Schuler D., Zarivach R.;
RT "Cation diffusion facilitators transport initiation and regulation is
RT mediated by cation induced conformational changes of the cytoplasmic
RT domain.";
RL PLoS ONE 9:E92141-E92141(2014).
RN [12] {ECO:0007744|PDB:5HSP}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 215-318, FUNCTION, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF MET-250.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=27550551; DOI=10.1038/srep31933;
RA Barber-Zucker S., Uebe R., Davidov G., Navon Y., Sherf D., Chill J.H.,
RA Kass I., Bitton R., Schuler D., Zarivach R.;
RT "Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein
RT MamM Causes Single-Domain Structural Loss and Signifies Its Importance.";
RL Sci. Rep. 6:31933-31933(2016).
RN [13] {ECO:0007744|PDB:6G55, ECO:0007744|PDB:6G5E, ECO:0007744|PDB:6G64, ECO:0007744|PDB:6G6I}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 215-318, FUNCTION, PROBABLE
RP IRON-BINDING, SUBUNIT, AND MUTAGENESIS OF 249-ASP--HIS-285 AND
RP 264-HIS--GLU-289.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=30811856; DOI=10.1111/febs.14795;
RA Barber-Zucker S., Hall J., Mangapuram S.V., Kass I., Kolusheva S.,
RA MacMillan F., Zarivach R., Henn A.;
RT "Metal binding to the dynamic cytoplasmic domain of the cation diffusion
RT facilitator (CDF) protein MamM induces a 'locked-in' configuration.";
RL FEBS J. 286:2193-2215(2019).
CC -!- FUNCTION: Essential for magnetosome formation; required for stable
CC accumulation of MamB (PubMed:22007638). May nucleate iron crystal
CC formation (Probable). Probably binds and transports iron. Binds
CC divalent cations, possibly up to 3 Zn(2+) per dimer in vitro, probably
CC iron in vivo (Probable) (PubMed:30811856). One of 7 genes (mamLQBIEMO)
CC able to induce magnetosome membrane biogenesis; coexpression of
CC mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores
CC magnetosome vesicle formation but not magnetite biosynthesis
CC (PubMed:27286560). {ECO:0000269|PubMed:22007638,
CC ECO:0000269|PubMed:27286560, ECO:0000269|PubMed:30811856,
CC ECO:0000305|PubMed:22007638, ECO:0000305|PubMed:24658343,
CC ECO:0000305|PubMed:24819161}.
CC -!- SUBUNIT: Forms homodimers via its C-terminal domain (CTD) in the
CC presence of metal cations (Probable). Interacts with MamB via their CTD
CC (PubMed:22007638, PubMed:29243866) (Probable). Isolated CTD forms
CC homodimers (PubMed:24658343, PubMed:24819161, PubMed:27550551,
CC PubMed:30811856). {ECO:0000269|PubMed:22007638,
CC ECO:0000269|PubMed:24658343, ECO:0000269|PubMed:24819161,
CC ECO:0000269|PubMed:27550551, ECO:0000269|PubMed:29243866,
CC ECO:0000269|PubMed:30811856, ECO:0000305|PubMed:22007638,
CC ECO:0000305|PubMed:24658343, ECO:0000305|PubMed:24819161}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:14766587, ECO:0000269|PubMed:22007638}; Multi-pass
CC membrane protein {ECO:0000255}. Cell inner membrane
CC {ECO:0000305|PubMed:22007638}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes with magnetosomes in a straight line
CC running through the center of the cell. {ECO:0000269|PubMed:22007638}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- DOMAIN: The C-terminal domain (CTD) is probably responsible for
CC hetero- and homodimerization; it assumes a V-shaped, dimeric metallo-
CC chaperone-like fold that can open and close. Val-260 forms the hinge
CC between the dimers. Binds up to 3 divalent metal cations (probably iron
CC in vivo); upon binding there is a conformational shift to a tighter
CC dimer (PubMed:24658343, PubMed:30811856) (Probable). If the CTD cannot
CC fold correctly the function of the whole protein is decreased,
CC suggesting the CTD confers functionality on the transmembrane domain
CC (TMD), perhaps activated by ligand binding to the CTD (Probable).
CC {ECO:0000269|PubMed:24658343, ECO:0000269|PubMed:30811856,
CC ECO:0000305|PubMed:24658343, ECO:0000305|PubMed:24819161,
CC ECO:0000305|PubMed:27550551}.
CC -!- DISRUPTION PHENOTYPE: Single gene disruption has no growth defects, no
CC accumulation of magnetite, forms empty intracellular magnetosome
CC vesicles, decreased levels of MamB, mislocation of MamC in 1-3 foci or
CC rarely in a shortened chain (PubMed:22007638). Magnetosome vesicles are
CC fewer and smaller, aligned in a chain with the filament, only a few
CC have very small crystals. Other, possibly precursor magnetosome
CC vesicles are visible. MamI mislocalized to cell inner membrane or in 1
CC to a few patches (PubMed:27286560). Deletion of approximately 80 kb of
CC DNA, 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:22007638,
CC ECO:0000269|PubMed:27286560}.
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 -!- 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 -!- MISCELLANEOUS: Cation diffusion facilitator (CDF) transporters all have
CC similar domain structure. By recreating in MamM mutations known in
CC paralogous human zinc transporters (Znt-8, SLC30A8 and ZnT-10,
CC SLC30A10), information about the effects of these mutations can be
CC learned. {ECO:0000303|PubMed:24819161, ECO:0000303|PubMed:27550551}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. {ECO:0000305|PubMed:22007638}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A sense of direction - Issue
CC 217 of September 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/217/";
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DR EMBL; BX571797; CAE12036.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78027.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30120.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99590.1; -; Genomic_DNA.
DR PDB; 3W5X; X-ray; 1.60 A; A=215-318.
DR PDB; 3W5Y; X-ray; 1.95 A; A/B=215-318.
DR PDB; 3W5Z; X-ray; 1.66 A; A=215-318.
DR PDB; 3W60; X-ray; 1.82 A; A=215-318.
DR PDB; 3W61; X-ray; 1.59 A; A=215-318.
DR PDB; 3W62; X-ray; 1.64 A; A=215-318.
DR PDB; 3W63; X-ray; 1.90 A; A=215-293.
DR PDB; 3W64; X-ray; 2.85 A; A/B/C/D=215-293.
DR PDB; 3W65; X-ray; 2.37 A; A=215-318.
DR PDB; 3W66; X-ray; 2.05 A; A=215-318.
DR PDB; 3W8G; X-ray; 2.05 A; A/B=215-318.
DR PDB; 3W8P; X-ray; 1.80 A; A/B=215-318.
DR PDB; 5HSP; X-ray; 1.79 A; A/D=215-318.
DR PDB; 6G55; X-ray; 1.65 A; A/D=215-318.
DR PDB; 6G5E; X-ray; 1.60 A; A=215-318.
DR PDB; 6G64; X-ray; 1.90 A; A=215-318.
DR PDB; 6G6I; X-ray; 2.40 A; A/B=215-318.
DR PDB; 6GMT; X-ray; 1.59 A; A=215-318.
DR PDB; 6GMV; X-ray; 1.59 A; A=215-318.
DR PDB; 6GP6; X-ray; 2.15 A; A/B=215-318.
DR PDB; 6H5K; X-ray; 1.54 A; A=215-318.
DR PDB; 6H5M; X-ray; 1.60 A; A=215-318.
DR PDB; 6H5U; X-ray; 2.00 A; A/B/C/H=215-318.
DR PDB; 6H5V; X-ray; 1.49 A; A=215-318.
DR PDB; 6H81; X-ray; 1.50 A; A=215-318.
DR PDB; 6H83; X-ray; 1.50 A; A=215-318.
DR PDB; 6H84; X-ray; 2.04 A; A=215-318.
DR PDB; 6H85; X-ray; 2.00 A; A=215-318.
DR PDB; 6H87; X-ray; 1.50 A; A=215-318.
DR PDB; 6H88; X-ray; 1.50 A; A=215-318.
DR PDB; 6H89; X-ray; 1.70 A; A=215-318.
DR PDB; 6H8A; X-ray; 1.80 A; A=215-318.
DR PDB; 6H8D; X-ray; 1.62 A; A=215-318.
DR PDB; 6H8G; X-ray; 1.35 A; A=215-318.
DR PDB; 6H8I; X-ray; 1.40 A; A=215-318.
DR PDB; 6H9P; X-ray; 2.10 A; A/B/C=215-318.
DR PDB; 6H9Q; X-ray; 1.50 A; A=215-318.
DR PDB; 6H9T; X-ray; 1.70 A; A=215-318.
DR PDB; 6HA2; X-ray; 1.50 A; A=215-318.
DR PDB; 6HAN; X-ray; 2.60 A; A/B/C/D=215-318.
DR PDB; 6HAO; X-ray; 2.40 A; A=215-318.
DR PDB; 6HHS; X-ray; 2.70 A; A/B/C/D/E/F/G=215-318.
DR PDBsum; 3W5X; -.
DR PDBsum; 3W5Y; -.
DR PDBsum; 3W5Z; -.
DR PDBsum; 3W60; -.
DR PDBsum; 3W61; -.
DR PDBsum; 3W62; -.
DR PDBsum; 3W63; -.
DR PDBsum; 3W64; -.
DR PDBsum; 3W65; -.
DR PDBsum; 3W66; -.
DR PDBsum; 3W8G; -.
DR PDBsum; 3W8P; -.
DR PDBsum; 5HSP; -.
DR PDBsum; 6G55; -.
DR PDBsum; 6G5E; -.
DR PDBsum; 6G64; -.
DR PDBsum; 6G6I; -.
DR PDBsum; 6GMT; -.
DR PDBsum; 6GMV; -.
DR PDBsum; 6GP6; -.
DR PDBsum; 6H5K; -.
DR PDBsum; 6H5M; -.
DR PDBsum; 6H5U; -.
DR PDBsum; 6H5V; -.
DR PDBsum; 6H81; -.
DR PDBsum; 6H83; -.
DR PDBsum; 6H84; -.
DR PDBsum; 6H85; -.
DR PDBsum; 6H87; -.
DR PDBsum; 6H88; -.
DR PDBsum; 6H89; -.
DR PDBsum; 6H8A; -.
DR PDBsum; 6H8D; -.
DR PDBsum; 6H8G; -.
DR PDBsum; 6H8I; -.
DR PDBsum; 6H9P; -.
DR PDBsum; 6H9Q; -.
DR PDBsum; 6H9T; -.
DR PDBsum; 6HA2; -.
DR PDBsum; 6HAN; -.
DR PDBsum; 6HAO; -.
DR PDBsum; 6HHS; -.
DR AlphaFoldDB; V6F235; -.
DR SMR; V6F235; -.
DR STRING; 1430440.MGMSRv2_2375; -.
DR TCDB; 2.A.4.7.4; the cation diffusion facilitator (cdf) family.
DR EnsemblBacteria; CDK99590; CDK99590; MGMSRv2__2375.
DR KEGG; mgry:MSR1_03400; -.
DR KEGG; mgy:MGMSRv2__2375; -.
DR eggNOG; COG0053; Bacteria.
DR HOGENOM; CLU_013430_3_6_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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1510.10; -; 1.
DR Gene3D; 3.30.70.1350; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027470; Cation_efflux_CTD.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR Pfam; PF16916; ZT_dimer; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biomineralization; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Ion transport; Iron; Iron transport;
KW Magnetosome; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..318
FT /note="Magnetosome protein MamM"
FT /id="PRO_0000447739"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..210
FT /note="Transmembrane domain (TMD)"
FT /evidence="ECO:0000305|PubMed:22007638"
FT REGION 211..318
FT /note="C-terminal domain (CTD)"
FT /evidence="ECO:0000305|PubMed:22007638"
FT BINDING 249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30811856"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:30811856"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30811856"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:30811856"
FT MUTAGEN 6..9
FT /note="CAVC->SAVS: Wild-type magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 9
FT /note="C->S: Wild-type magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 46
FT /note="Y->D: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 46
FT /note="Y->H: About 90% magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 50
FT /note="D->A: About 50% magnetic response, fewer cells have
FT iron crystals which are smaller, in addition to magnetite
FT (Fe(3)O(4)) crystals of hematite (Fe(2)O(3)) also form."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 139
FT /note="C->A: Wild-type magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 155
FT /note="H->A: About 65% magnetic response, fewer cells have
FT iron crystals which are larger."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 159
FT /note="D->A: About 55% magnetic response, fewer cells have
FT iron crystals which have altered morphology."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 249..285
FT /note="DMIIGVDPENTVEQAHEICEAVQAAVCGKIRRIESLH->AMIIGVDPENTVE
FT QAHEICEAVQAAVCGKIRRIESLA: CTD binds only 2 cations."
FT /evidence="ECO:0000269|PubMed:30811856"
FT MUTAGEN 249
FT /note="D->A: Slightly decreased wild-type magnetic
FT response, fewer, slightly smaller magnetite crystals.
FT Significantly decreased magnetic response, many fewer,
FT smaller crystals in vivo, isolated CTD does not bind
FT cations; when associated with A-264."
FT /evidence="ECO:0000269|PubMed:24658343"
FT MUTAGEN 250
FT /note="M->L: CTD behaves like wild-type."
FT /evidence="ECO:0000269|PubMed:27550551"
FT MUTAGEN 250
FT /note="M->P: Severely impaired magnetic response, cells
FT make very few, small magnetite particles, less MamB and
FT MamM protein accumulate. CTD no longer dimerizes, CTD has
FT cannot fold properly and is unstable."
FT /evidence="ECO:0000269|PubMed:27550551"
FT MUTAGEN 259..318
FT /note="Missing: Loss of magnetic response, reduces MamB
FT expression."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 260
FT /note="V->G: Nearly wild-type magnetic response."
FT /evidence="ECO:0000269|PubMed:24819161"
FT MUTAGEN 260
FT /note="V->P: CTD dimerizes, binds fewer cations. Loss of
FT magnetic response, still stabilizes MamB."
FT /evidence="ECO:0000269|PubMed:24658343,
FT ECO:0000269|PubMed:24819161"
FT MUTAGEN 260
FT /note="V->R: Loss of magnetic response, still stabilizes
FT MamB, CTD dimerizes, binds cations, dimer interface is
FT tighter and twisted."
FT /evidence="ECO:0000269|PubMed:24819161"
FT MUTAGEN 260
FT /note="V->W: Significantly reduced magnetic response, many
FT fewer, much smaller magnetite crystals formed, still
FT stabilizes MamB, CTD dimerizes, binds fewer cations."
FT /evidence="ECO:0000269|PubMed:24819161"
FT MUTAGEN 264..289
FT /note="HEICEAVQAAVCGKIRRIESLHVSAE->AEICEAVQAAVCGKIRRIESLHVS
FT AA: CTD binds only 1 cation."
FT /evidence="ECO:0000269|PubMed:30811856"
FT MUTAGEN 264
FT /note="H->A: Wild-type magnetic response, no change in
FT magnetite crystal size, number or shape. Significantly
FT decreased magnetic response, many fewer, smaller crystals
FT in vivo, isolated CTD does not bind cations; when
FT associated with A-249."
FT /evidence="ECO:0000269|PubMed:24658343"
FT MUTAGEN 285
FT /note="H->A: Wild-type magnetic response, no change in
FT magnetite crystal size, number or shape."
FT /evidence="ECO:0000269|PubMed:24658343"
FT MUTAGEN 289..318
FT /note="Missing: Wild-type magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 289
FT /note="E->A: Nearly wild-type magnetic response, fewer
FT magnetite crystals of normal size and shape."
FT /evidence="ECO:0000269|PubMed:24658343"
FT MUTAGEN 309..318
FT /note="Missing: Wild-type magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:6H8G"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:6H8G"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:6H8G"
FT HELIX 260..277
FT /evidence="ECO:0007829|PDB:6H8G"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:6H8G"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3W8G"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:6G55"
SQ SEQUENCE 318 AA; 34485 MW; 76939A4A3FBCE291 CRC64;
MRKSGCAVCS RSIGWVGLAV STVLMVMKAF VGLIGGSQAM LADAMYSLKD MLNALMVIIG
TTISSKPLDA EHPYGHGKVE FILSMVVSVV FIVLTGYLLV HAVQILLDES LHRTPHLIVL
WAALVSIGVN VGMYFYSRCV AIETNSPLIK TMAKHHHGDA TASGAVALGI IGAHYLNMPW
IDPAVALWET IDLLLLGKVV FMDAYRGLMD HTAGEAVQNR IVEAAERVPG VRGVIHLRAR
YVGQDIWADM IIGVDPENTV EQAHEICEAV QAAVCGKIRR IESLHVSAEA REIGDTTKPS
FSDQPLSFDE VMLSKVDN
