MAMB_MAGSQ
ID MAMB_MAGSQ Reviewed; 293 AA.
AC W6KHH6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Magnetosome protein MamB {ECO:0000303|PubMed:29243866};
DE AltName: Full=Probable iron transporter MamB {ECO:0000305};
GN Name=mamB; ORFNames=MGMAQ_1061;
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira; unclassified Magnetospira.
OX NCBI_TaxID=1288970;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2;
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(2014).
RN [2] {ECO:0007744|PDB:5HO1, ECO:0007744|PDB:5HO3, ECO:0007744|PDB:5HO5}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 213-293 IN COMPLEX WITH ZINC,
RP FUNCTION, PROBABLE IRON-BINDING, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP ASP-247.
RC STRAIN=QH-2;
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 (By similarity). Probably binds and transports iron (Probable).
CC Requires heterodimerization with MamM for stability (By similarity).
CC {ECO:0000250|UniProtKB:V6F510, ECO:0000305|PubMed:29243866}.
CC -!- SUBUNIT: The isolated C-terminal domain (approximately 213-293) forms
CC homodimers (PubMed:29243866). Forms heterodimers with MamM (By
CC similarity). {ECO:0000250|UniProtKB:V6F510,
CC ECO:0000269|PubMed:29243866}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000250|UniProtKB:V6F510}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The C-terminal domain (CTD) forms a V-shaped, dimeric metallo-
CC chaperone-like fold and binds 1 metal cation (probably Fe in vivo,
CC structure determined with Zn(2+)) per subunit (PubMed:29243866). The
CC CTD is probably responsible for hetero- and homodimerization
CC (Probable). {ECO:0000269|PubMed:29243866, ECO:0000305|PubMed:29243866}.
CC -!- MISCELLANEOUS: This bacteria has on average 16 oval magnetosomes of
CC about 81 X 58 nm which contain membrane-bound crystals of magnetite
CC (Fe(3)O(4)). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. {ECO:0000305}.
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DR EMBL; FO538765; CCQ73001.1; -; Genomic_DNA.
DR RefSeq; WP_046020684.1; NZ_FO538765.1.
DR PDB; 5HO1; X-ray; 2.53 A; A/B=213-292.
DR PDB; 5HO3; X-ray; 2.15 A; A/B=213-293.
DR PDB; 5HO5; X-ray; 1.99 A; A/B/C/D=213-292.
DR PDB; 5HOK; X-ray; 1.70 A; A/B/C/D=213-293.
DR PDBsum; 5HO1; -.
DR PDBsum; 5HO3; -.
DR PDBsum; 5HO5; -.
DR PDBsum; 5HOK; -.
DR AlphaFoldDB; W6KHH6; -.
DR SMR; W6KHH6; -.
DR EnsemblBacteria; CCQ73001; CCQ73001; MGMAQ_1061.
DR KEGG; magq:MGMAQ_1061; -.
DR HOGENOM; CLU_013430_3_3_5; -.
DR OMA; TINQIMW; -.
DR OrthoDB; 381612at2; -.
DR Proteomes; UP000032733; 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 1: Evidence at protein level;
KW 3D-structure; Biomineralization; Ion transport; Iron; Iron transport;
KW Magnetosome; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc.
FT CHAIN 1..293
FT /note="Magnetosome protein MamB"
FT /id="PRO_0000447738"
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..78
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..158
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..293
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..293
FT /note="C-terminal domain (CTD)"
FT /evidence="ECO:0000305|PubMed:29243866"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29243866,
FT ECO:0007744|PDB:5HO1"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29243866,
FT ECO:0007744|PDB:5HO1"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29243866,
FT ECO:0007744|PDB:5HO1"
FT MUTAGEN 247
FT /note="D->A: Isolated CTD does not bind metal."
FT /evidence="ECO:0000269|PubMed:29243866"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:5HOK"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:5HOK"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:5HOK"
FT HELIX 258..275
FT /evidence="ECO:0007829|PDB:5HOK"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:5HOK"
SQ SEQUENCE 293 AA; 31446 MW; 7991BC19479A1631 CRC64;
MTTAACRKCR DEVIWWAFFI NIGQTTYKGV LGVLSGSAAL VADAMHSGAD VVATLVTMFS
VKVSDKKADE KYPFGYGNIQ FIASSIVGLI LFFGALYLMY ESTMQIIAGN TSSPSPFAVL
GAIVSIATNE LMFRYQSCVG RQNNSPAIIA NAWDNRSDAL SSVAVLIGIV AAVVGFPIAD
RLAAIGVGIL VAKIGIELNI DAINGLMDTS VENDVLVDAY NIAKDSQHVH GVHYIRGRNV
GEDVHLDINI YVDADLKVFE SDLVADAIRR KIEAEVDHVR DVHVGVTPVR IAA
