MAMP_MAGSA
ID MAMP_MAGSA Reviewed; 275 AA.
AC Q2W8Q1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Multi-heme protein MamP {ECO:0000305};
DE EC=1.-.-.- {ECO:0000269|PubMed:25775527};
DE AltName: Full=Magnetochrome MamP {ECO:0000305};
DE AltName: Full=Magnetosome-associated protein MamP {ECO:0000303|PubMed:23176475};
GN Name=mamP; OrderedLocusNames=amb0970;
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 POSSIBLE COFACTOR.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=23176475; DOI=10.1042/bst20120104;
RA Siponen M.I., Adryanczyk G., Ginet N., Arnoux P., Pignol D.;
RT "Magnetochrome: a c-type cytochrome domain specific to magnetotatic
RT bacteria.";
RL Biochem. Soc. Trans. 40:1319-1323(2012).
RN [4]
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).
RN [5]
RP DOMAIN.
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).
RN [6]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF
RP CYS-224 AND CYS-268.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=25048532; DOI=10.1111/1574-6968.12541;
RA Taoka A., Eguchi Y., Mise S., Oestreicher Z., Uno F., Fukumori Y.;
RT "A magnetosome-associated cytochrome MamP is critical for magnetite crystal
RT growth during the exponential growth phase.";
RL FEMS Microbiol. Lett. 358:21-29(2014).
RN [7]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION
RP PHENOTYPE, HEME-BINDING, AND MUTAGENESIS OF 224-CYS--HIS-228 AND
RP 268-CYS--HIS-272.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=25775527; DOI=10.1073/pnas.1417614112;
RA Jones S.R., Wilson T.D., Brown M.E., Rahn-Lee L., Yu Y., Fredriksen L.L.,
RA Ozyamak E., Komeili A., Chang M.C.;
RT "Genetic and biochemical investigations of the role of MamP in redox
RT control of iron biomineralization in Magnetospirillum magneticum.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3904-3909(2015).
RN [8]
RP PROTEOLYTIC CLEAVAGE, AND PROBABLE TOPOLOGY.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27302060; DOI=10.1074/jbc.m116.731000;
RA Hershey D.M., Browne P.J., Iavarone A.T., Teyra J., Lee E.H., Sidhu S.S.,
RA Komeili A.;
RT "Magnetite biomineralization in Magnetospirillum magneticum is regulated by
RT a switch-like behavior in the HtrA protease MamE.";
RL J. Biol. Chem. 291:17941-17952(2016).
RN [9]
RP PROTEOLYTIC CLEAVAGE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=26981620; DOI=10.1371/journal.pbio.1002402;
RA Hershey D.M., Ren X., Melnyk R.A., Browne P.J., Ozyamak E., Jones S.R.,
RA Chang M.C., Hurley J.H., Komeili A.;
RT "MamO is a repurposed serine protease that promotes magnetite
RT biomineralization through direct transition metal binding in magnetotactic
RT bacteria.";
RL PLoS Biol. 14:E1002402-E1002402(2016).
CC -!- FUNCTION: Involved in redox-control of magnetite formation; oxidizes
CC Fe(2+) to Fe(3+) or to mixed-valent Fe(2+)-Fe(3+) oxide minerals
CC (PubMed:25775527). May control magnetite crystal size and number
CC (Probable). Overproduction of MamP leads to more crystals than normal
CC during exponential growth of normal size; in stationary phase crystal
CC numbers become wild-type (PubMed:25048532).
CC {ECO:0000269|PubMed:25048532, ECO:0000269|PubMed:25775527,
CC ECO:0000305|PubMed:20212111}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:A0A1S7LCW6,
CC ECO:0000305|PubMed:25048532, ECO:0000305|PubMed:25775527};
CC Note=Binds 2 heme groups via the 2 magnetochrome (MCR) motifs.
CC {ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:25048532,
CC ECO:0000305|PubMed:25775527};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -89 +/- 11 mV for Fe(3+)-Fe(2+) at pH 7.5.
CC {ECO:0000269|PubMed:25775527};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:25775527}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:25048532}; Single-pass membrane protein
CC {ECO:0000305|PubMed:25048532}. Note=Not seen in magnetosome membranes.
CC {ECO:0000269|PubMed:25048532}.
CC -!- INDUCTION: Constitutively expressed, levels are high for 24 hours after
CC innoculation then decrease in stationary phase (up to 144 hours) (at
CC protein level) (PubMed:25048532). Part of the probable 18 gene mamAB
CC operon (Probable). {ECO:0000269|PubMed:25048532,
CC ECO:0000305|PubMed:20212111}.
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:0000250|UniProtKB:A0A1S7LCW6}.
CC -!- PTM: Subject to proteolytic cleavage which requires both MamE and MamO.
CC {ECO:0000269|PubMed:26981620, ECO:0000269|PubMed:27302060}.
CC -!- DISRUPTION PHENOTYPE: Cells have a weak magnetic response and make
CC magnetosome membranes. Has fewer but larger magnetite crystals
CC (PubMed:20212111). Makes small, flaky magnetite crystals, does not
CC alter subcellular localization of MamC, MamF, MamI or MmsF
CC (PubMed:25775527). Deletion of genes mamH to mamV (amb0961 to amb0978)
CC gives cells with no magnetosomes and no magnetic response
CC (PubMed:20212111). {ECO:0000269|PubMed:20212111,
CC ECO:0000269|PubMed:25775527}.
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 magnetosome MamP family. {ECO:0000305}.
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DR EMBL; AP007255; BAE49774.1; -; Genomic_DNA.
DR RefSeq; WP_011383401.1; NC_007626.1.
DR AlphaFoldDB; Q2W8Q1; -.
DR SMR; Q2W8Q1; -.
DR EnsemblBacteria; BAE49774; BAE49774; amb0970.
DR KEGG; mag:amb0970; -.
DR HOGENOM; CLU_1029742_0_0_5; -.
DR OMA; GACHAII; -.
DR OrthoDB; 884654at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IPR036034; PDZ_sf.
DR Pfam; PF18509; MCR; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell inner membrane; Cell membrane; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..275
FT /note="Multi-heme protein MamP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000447783"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..20
FT /evidence="ECO:0000305|PubMed:24097349"
FT TOPO_DOM 21..275
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27302060"
FT REGION 89..206
FT /note="PDZ"
FT /evidence="ECO:0000305|PubMed:24097349"
FT MOTIF 210..230
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:24097349"
FT MOTIF 250..274
FT /note="MCR 2"
FT /evidence="ECO:0000305|PubMed:24097349"
FT BINDING 224
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6,
FT ECO:0000305|PubMed:23176475"
FT BINDING 227
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6,
FT ECO:0000305|PubMed:23176475"
FT BINDING 228
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:0000250|UniProtKB:A0A1S7LCW6,
FT ECO:0000305|PubMed:23176475"
FT BINDING 268
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6,
FT ECO:0000305|PubMed:23176475"
FT BINDING 271
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:A0A1S7LCW6,
FT ECO:0000305|PubMed:23176475"
FT BINDING 272
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:0000250|UniProtKB:A0A1S7LCW6,
FT ECO:0000305|PubMed:23176475"
FT MUTAGEN 224..228
FT /note="CTDCH->ATDAA: Loss of magnetic response, no
FT restoration of magnetite particle size."
FT /evidence="ECO:0000269|PubMed:25775527"
FT MUTAGEN 224
FT /note="C->A: No heme binding, makes smaller magnetite
FT crystals; when associated with A-268."
FT /evidence="ECO:0000269|PubMed:25048532"
FT MUTAGEN 268..272
FT /note="CEACH->AEAAA: Loss of magnetic response, no
FT restoration of magnetite particle size."
FT /evidence="ECO:0000269|PubMed:25775527"
FT MUTAGEN 268
FT /note="C->A: No heme binding, makes smaller magnetite
FT crystals; when associated with A-224."
FT /evidence="ECO:0000269|PubMed:25048532"
SQ SEQUENCE 275 AA; 28912 MW; E43A5005E85721A9 CRC64;
MNSKVALLVV GLAVVLALVI GRQGPVAPQA TNTQSQAVAA GPVAAPVAFP QPLYPQAANV
AMPVEPDPAA GGGTAPATES PLPNFVPRKL KVFEGHWQGM DGRLMTEELA RKLNYPRGLQ
GVLLGEVTLN AAFSGLLAGD LIVRIDDTPV TDMESFKAAS RTVANRSDAR ISVLRKDNRP
GAPVVRKLTV VLREAEGGLG FAQLEGAPMI LAGDPRPHGY RGACTDCHPI GQGFELTPDP
DLISLPPPTI TRDMVARSVN PHEVRGPCEA CHVIK
