MAMB_MAGGM
ID MAMB_MAGGM Reviewed; 297 AA.
AC V6F510; Q6NE50; Q93DY6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Magnetosome protein MamB {ECO:0000305};
DE AltName: Full=MM33.3 {ECO:0000303|PubMed:11571158};
DE AltName: Full=Probable iron transporter MamB {ECO:0000305};
GN Name=mamB {ECO:0000303|PubMed:11571158}; OrderedLocusNames=MGMSRv2__2368;
GN ORFNames=mgI499, MGR_4102;
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 1-21, AND
RP 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 1-12, 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, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-6; CYS-9; HIS-46; ASP-50; CYS-138; ASP-154; ASP-158;
RP 288-PRO--VAL-297 AND 293-VAL--VAL-297.
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 [8]
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 [9]
RP FUNCTION, MINIMAL VESICLE FORMATION GENES, DEVELOPMENTAL STAGE, AND
RP 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 [10]
RP FUNCTION, MINIMAL VESICLE FORMATION GENES, SUBUNIT, DISRUPTION PHENOTYPE,
RP DOMAIN, AND MUTAGENESIS OF ASP-247.
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: Plays a dual, essential role in magnetosome formation;
CC required for magnetosome vesicle formation as well as biomineralization
CC (Probable) (PubMed:29243866). Requires heterodimerization with MamM for
CC stability (PubMed:22007638). Probably binds and transports iron
CC (Probable). One of 7 genes (mamLQBIEMO) able to induce magnetosome
CC membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the
CC 17 gene mamAB operon restores magnetosome vesicle formation but not
CC magnetite biosynthesis (PubMed:27286560). {ECO:0000269|PubMed:22007638,
CC ECO:0000269|PubMed:27286560, ECO:0000269|PubMed:29243866,
CC ECO:0000305|PubMed:22007638, ECO:0000305|PubMed:29243866}.
CC -!- SUBUNIT: Forms homodimers via its C-terminal domain, may form higher
CC order multimers that are sensitive to reducing agent. Probably
CC interacts with MamE (Probable). Interacts with MamM via their C-
CC terminal domains (PubMed:22007638, PubMed:29243866).
CC {ECO:0000269|PubMed:22007638, ECO:0000269|PubMed:29243866,
CC ECO:0000305|PubMed:22007638}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:22007638}; Multi-pass membrane protein
CC {ECO:0000255}. Magnetosome membrane {ECO:0000269|PubMed:11571158,
CC ECO:0000269|PubMed:14766587, ECO:0000269|PubMed:22007638}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Purified magnetosomes remain
CC attached to each other (PubMed:11571158). Tagged protein has several
CC locations; most is in 1-3 dots in the cell, also seen as patchy
CC membrane localization, while about 20% localizes with magnetosomes in a
CC straight line running through the center of the cell (PubMed:22007638).
CC {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:22007638}.
CC -!- DEVELOPMENTAL STAGE: Upon induction in a non-magnetic deletion mutant
CC this protein is first found in the cell inner membrane, then collects
CC into foci along the entire cell length from which magnetosome vesicle
CC formation and subsequent clustering occur (at protein level).
CC {ECO:0000269|PubMed:27286560}.
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 and binds 1 Fe cation per subunit
CC (Probable). The CTD assumes a V-shaped, dimeric metallo-chaperone-like
CC fold (By similarity). {ECO:0000250|UniProtKB:W6KHH6,
CC ECO:0000305|PubMed:29243866}.
CC -!- DISRUPTION PHENOTYPE: The most severe single mam gene deletion. Single
CC gene disruption has no accumulation of magnetite, no intracellular
CC magnetosome vesicles form, wild type levels of MamM, mislocation of
CC MamC in 1-3 foci, MamI mislocalized in 1 to a few patches
CC (PubMed:22007638, PubMed:27286560, PubMed:29243866). Deletion of
CC approximately 80 kb of DNA, including this operon, leads to cells that
CC are non-magnetic, lack internal membrane systems, grow poorly, have
CC reduced mobility and take-up and accumulate iron poorly
CC (PubMed:13129949). {ECO:0000269|PubMed:13129949,
CC ECO:0000269|PubMed:22007638, ECO:0000269|PubMed:27286560,
CC ECO:0000269|PubMed:29243866}.
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 -!- 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 -!- 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; AF374354; AAL09999.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12043.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30127.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78034.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99583.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F510; -.
DR SMR; V6F510; -.
DR STRING; 1430440.MGMSRv2_2368; -.
DR TCDB; 2.A.4.7.3; the cation diffusion facilitator (cdf) family.
DR EnsemblBacteria; CDK99583; CDK99583; MGMSRv2__2368.
DR KEGG; mgy:MGMSRv2__2368; -.
DR eggNOG; COG0053; Bacteria.
DR HOGENOM; CLU_013430_3_3_5; -.
DR OrthoDB; 381612at2; -.
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 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..297
FT /note="Magnetosome protein MamB"
FT /id="PRO_0000447736"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..83
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..164
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..214
FT /note="Transmembrane domain (TMD)"
FT /evidence="ECO:0000305|PubMed:29243866"
FT REGION 215..297
FT /note="C-terminal domain (CTD)"
FT /evidence="ECO:0000305|PubMed:29243866"
FT MUTAGEN 6
FT /note="C->S: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 9
FT /note="C->S: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 46
FT /note="H->A: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 50
FT /note="D->A: Loss of magnetic response. MamD is correctly
FT localized, magnetosome vesicles form but are empty."
FT /evidence="ECO:0000269|PubMed:22007638,
FT ECO:0000269|PubMed:29243866"
FT MUTAGEN 50
FT /note="D->E: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 138
FT /note="C->A: Loss of magnetic response, decreased protein
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 154
FT /note="D->A: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 158
FT /note="D->A: Loss of magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 247
FT /note="D->A: About 30% fewer magnetite particles per cell,
FT their size is normal."
FT /evidence="ECO:0000269|PubMed:29243866"
FT MUTAGEN 288..297
FT /note="Missing: About 60% magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT MUTAGEN 293..297
FT /note="Missing: About 40% magnetic response."
FT /evidence="ECO:0000269|PubMed:22007638"
FT CONFLICT 193
FT /note="H -> R (in Ref. 1; AAL09999/CAJ30127 and 4;
FT CAM78034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 31942 MW; 1D03291B50B341FA CRC64;
MKFENCRDCR EEVVWWAFTA DICMTLFKGI LGLMSGSVAL VADSLHSGAD VVASGVTQLS
LKISNKPADE RYPFGYGNIQ YISSAIVGSL LLIGASFLMY GSVVKLISGT YEAPSIFAAL
GASVTVIVNE LMYRYQICVG NENNSPAIIA NAWDNRSDAI SSAAVMVGVI ASVIGFPIAD
TIAAIGVSAL VGHIGLELIG KAVHGLMDSS VDTELLQTAW QIATDTPLVH SIYFLRGRHV
GEDVQFDIRL RVDPNLRIKD SSMVAEAVRQ RIQDEIPHAR DIRLFVSPAP AAVTVRV
