MAMP_MAGMO
ID MAMP_MAGMO Reviewed; 260 AA.
AC A0A1S7LCW6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Multi-heme protein MamP {ECO:0000305};
DE EC=1.-.-.- {ECO:0000269|PubMed:24097349};
DE AltName: Full=Magnetochrome MamP {ECO:0000305};
DE AltName: Full=Magnetosome-associated protein MamP {ECO:0000303|PubMed:24097349};
GN Name=mamP; ORFNames=MAGMO_0521;
OS Magnetococcus massalia (strain MO-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=451514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MO-1;
RX PubMed=27902881; DOI=10.1111/1462-2920.13637;
RA Ji B., Zhang S.D., Zhang W.J., Rouy Z., Alberto F., Santini C.L.,
RA Mangenot S., Gagnot S., Philippe N., Pradel N., Zhang L., Tempel S., Li Y.,
RA Medigue C., Henrissat B., Coutinho P.M., Barbe V., Talla E., Wu L.F.;
RT "The chimeric nature of the genomes of marine magnetotactic coccoid-ovoid
RT bacteria defines a novel group of Proteobacteria.";
RL Environ. Microbiol. 19:1103-1119(2017).
RN [2] {ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-260 IN COMPLEX WITH HEME,
RP FUNCTION, COFACTOR, SUBUNIT, DOMAIN, HEME-BINDING, IRON-BINDING, AND
RP MUTAGENESIS OF 91-GLU--GLU-98; GLU-123; GLU-193 AND 227-ASP--ASP-229.
RC STRAIN=MO-1;
RX PubMed=24097349; DOI=10.1038/nature12573;
RA Siponen M.I., Legrand P., Widdrat M., Jones S.R., Zhang W.J., Chang M.C.,
RA Faivre D., Arnoux P., Pignol D.;
RT "Structural insight into magnetochrome-mediated magnetite
RT biomineralization.";
RL Nature 502:681-684(2013).
CC -!- FUNCTION: Oxidizes Fe(2+) at alkaline pH; successively forms
CC ferrihydrite (Fe(3+)(2)O(3) 0.5 H(2)O) then magnetite (Fe(3)O(4)) from
CC an Fe(2+) solution. {ECO:0000269|PubMed:24097349}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:24097349};
CC Note=Binds 2 heme groups via the magnetochrome (MCR) motifs.
CC {ECO:0000269|PubMed:24097349};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0 for oxidation of Fe(2+).
CC {ECO:0000269|PubMed:24097349};
CC -!- SUBUNIT: Exists in a homodimer-homotetramer equilibrium.
CC {ECO:0000269|PubMed:24097349}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q2W8Q1}; Single-pass membrane protein
CC {ECO:0000305|PubMed:24097349}. Note=Not seen in magnetosome membranes.
CC {ECO:0000250|UniProtKB:Q2W8Q1}.
CC -!- DOMAIN: The dimer forms a pocket of about 8 X 15 Angstroms, lined with
CC acidic residues, which may bind 2 Fe(2+) ions.
CC {ECO:0000269|PubMed:24097349}.
CC -!- PTM: Subject to proteolytic cleavage which requires both MamE and MamO.
CC {ECO:0000250|UniProtKB:Q2W8Q1}.
CC -!- MISCELLANEOUS: This bacteria has on average 17 elongated cubo-
CC octahedral shaped magnetosome with a size of 64 X 57 nm which contain
CC membrane-bound crystals of magnetite (Fe(3)O(4)). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the magnetosome MamP family. {ECO:0000305}.
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DR EMBL; LO017727; CRH04725.1; -; Genomic_DNA.
DR PDB; 4JJ0; X-ray; 1.80 A; A/B=26-260.
DR PDB; 4JJ3; X-ray; 2.80 A; A/B=26-260.
DR PDBsum; 4JJ0; -.
DR PDBsum; 4JJ3; -.
DR AlphaFoldDB; A0A1S7LCW6; -.
DR SMR; A0A1S7LCW6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR040963; MCR.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF18509; MCR; 2.
DR Pfam; PF13180; PDZ_2; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biomineralization; Cell inner membrane; Cell membrane; Heme;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..260
FT /note="Multi-heme protein MamP"
FT /id="PRO_0000447784"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..21
FT /evidence="ECO:0000305|PubMed:24097349"
FT TOPO_DOM 22..260
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 86..194
FT /note="PDZ"
FT /evidence="ECO:0000305|PubMed:24097349"
FT MOTIF 195..218
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:24097349"
FT MOTIF 238..258
FT /note="MCR 2"
FT /evidence="ECO:0000305|PubMed:24097349"
FT BINDING 206
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 212
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 215
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 216
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 246
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 252
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 255
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT BINDING 256
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:24097349,
FT ECO:0007744|PDB:4JJ0, ECO:0007744|PDB:4JJ3"
FT MUTAGEN 91..98
FT /note="EAHWQGME->AAAWQGMA: Loss of magnetic response and
FT magnetite formation; when associated with A-123, A-193 and
FT 227-A--A-229."
FT /evidence="ECO:0000269|PubMed:24097349"
FT MUTAGEN 123
FT /note="E->A: Loss of magnetic response and magnetite
FT formation; when associated with 91-A--A-98, A-193 and 227-
FT A--A-229."
FT /evidence="ECO:0000269|PubMed:24097349"
FT MUTAGEN 193
FT /note="E->A: Loss of magnetic response and magnetite
FT formation; when associated with 91-A--A-98, A-123 and 227-
FT A--A-229."
FT /evidence="ECO:0000269|PubMed:24097349"
FT MUTAGEN 227..229
FT /note="DPD->APA: Loss of magnetic response and magnetite
FT formation; when associated with 91-A--A-98, A-123 and A-
FT 193."
FT /evidence="ECO:0000269|PubMed:24097349"
SQ SEQUENCE 260 AA; 27638 MW; B2CF0D7F9FB5B55F CRC64;
MKLKGTTIVA LGMLVVAIMV LASMIDLPGS DMSATPAPPD TPRGAPIVGG QGQAMGLPVA
MQRRRGEQRA PVPALSDANG GFVAPNVQFS EAHWQGMEAL PLSIELKRKL KLPLDLEGLL
IDETSLNAAV SGLLAGDVLV AINGRKVKTL KKMQKETRRV QMDRRASLTV YRKGRLLTLT
LSEEKNLGLA QVETAPMILP GDIMPHPYRG PCTQCHAIGT TGHITPDPDG IVLPPGPIRA
GAKMPHRDRG PCAACHAIIQ
