MAMB_MAGSA
ID MAMB_MAGSA Reviewed; 296 AA.
AC Q2W8L4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Magnetosome protein MamB {ECO:0000305};
DE AltName: Full=Probable iron transporter MamB {ECO:0000305};
GN Name=mamB; OrderedLocusNames=amb0974, amb1007;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
RN [2]
RP FUNCTION, PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20212111; DOI=10.1073/pnas.0914439107;
RA Murat D., Quinlan A., Vali H., Komeili A.;
RT "Comprehensive genetic dissection of the magnetosome gene island reveals
RT the step-wise assembly of a prokaryotic organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5593-5598(2010).
RN [3]
RP MINIMAL MAGNETOSOME ISLAND.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=22716969; DOI=10.1111/j.1365-2958.2012.08132.x;
RA Murat D., Falahati V., Bertinetti L., Csencsits R., Koernig A., Downing K.,
RA Faivre D., Komeili A.;
RT "The magnetosome membrane protein, MmsF, is a major regulator of magnetite
RT biomineralization in Magnetospirillum magneticum AMB-1.";
RL Mol. Microbiol. 85:684-699(2012).
CC -!- FUNCTION: Plays a dual, essential role in magnetosome formation;
CC required for magnetosome vesicle formation as well as biomineralization
CC (PubMed:20212111) (Probable). Probably binds and transports iron (By
CC similarity). Requires heterodimerization with MamM for stability (By
CC similarity). {ECO:0000250|UniProtKB:V6F510,
CC ECO:0000269|PubMed:20212111, ECO:0000305|PubMed:20212111}.
CC -!- SUBUNIT: Forms heterodimers with MamM (By similarity). Probably
CC interacts with MamE (By similarity). {ECO:0000250|UniProtKB:V6F510}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000250|UniProtKB:V6F510}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Locus amb0974 is part of the probable 18 gene mamAB operon.
CC {ECO:0000305|PubMed:20212111}.
CC -!- DOMAIN: The C-terminal domain (CTD) is probably responsible for
CC hetero- and homodimerization (By similarity). The CTD assumes a V-
CC shaped, dimeric metallo-chaperone-like fold and binds 1 Fe cation per
CC subunit (By similarity). {ECO:0000250|UniProtKB:V6F510,
CC ECO:0000250|UniProtKB:W6KHH6}.
CC -!- DISRUPTION PHENOTYPE: When both copies of this protein are deleted
CC cells have no magnetic response and no magnetosome membranes. Deletion
CC of just amb0974 leads to an intermediate magnetic response and still
CC makes magnetosome membranes (PubMed:20212111). Deletion of genes mamH
CC to mamV (amb0961 to amb0978) gives cells with no magnetosomes and no
CC magnetic response (PubMed:20212111). {ECO:0000269|PubMed:20212111}.
CC -!- MISCELLANEOUS: This bacteria makes up to 20 cubo-octahedral
CC magnetosomes of about 45 nm in diameter which contain membrane-bound
CC crystals of magnetite (Fe(3)O(4)). {ECO:0000305}.
CC -!- MISCELLANEOUS: Expression of just the minimal mamAB gene cluster
CC (amb0961 to amb0978), including this gene, is sufficient to form a
CC minimal magnetosome chain with small magnetite particles.
CC {ECO:0000269|PubMed:22716969}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. {ECO:0000305}.
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DR EMBL; AP007255; BAE49778.1; -; Genomic_DNA.
DR EMBL; AP007255; BAE49811.1; -; Genomic_DNA.
DR RefSeq; WP_008622631.1; NC_007626.1.
DR AlphaFoldDB; Q2W8L4; -.
DR SMR; Q2W8L4; -.
DR EnsemblBacteria; BAE49778; BAE49778; amb0974.
DR EnsemblBacteria; BAE49811; BAE49811; amb1007.
DR KEGG; mag:amb0974; -.
DR KEGG; mag:amb1007; -.
DR HOGENOM; CLU_013430_3_3_5; -.
DR OMA; TINQIMW; -.
DR OrthoDB; 381612at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110146; C:magnetosome membrane; ISS:UniProtKB.
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 3: Inferred from homology;
KW Biomineralization; Ion transport; Iron; Iron transport; Magnetosome;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..296
FT /note="Magnetosome protein MamB"
FT /id="PRO_0000447737"
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..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..214
FT /note="Transmembrane domain (TMD)"
FT /evidence="ECO:0000305"
FT REGION 215..296
FT /note="C-terminal domain (CTD)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 31875 MW; EAC0B685CE70B2EE CRC64;
MKFENCRDCR EEVVWWAFTA DICMTLFKGV LGLMSGSVAL VADSLHSGAD VVASGVTQLS
LKISNKPADE RYPFGYGNIQ YISSSIVGSL LLIGASFLMY GSVMKLISGT YEAPSIFAAV
GASVTVIVNE LMYRYQICVG NENNSPAIIA NAWDNRSDAI SSAAVMVGVI ASVIGFPIAD
TIAAIGVSAL VGRIGLELIG TSIHGLMDSS VDTELLQTAW QVAMDTPMVH SIYFLRGRHV
GEDVQFDIRL RVDPNLRIKD SSMVAEAVRR RIQEEIPHAR DIRLFVSPAP AAAARA
