MAMP_MAGGM
ID MAMP_MAGGM Reviewed; 270 AA.
AC Q93DZ0; V6F2H3;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Multi-heme protein MamP {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Magnetochrome MamP {ECO:0000303|PubMed:23176475};
DE AltName: Full=Magnetosome-associated protein MamP;
GN Name=mamP {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2372;
GN ORFNames=mgI494, MGR_4098;
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].
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 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 [7]
RP POSSIBLE COFACTOR.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
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 [8]
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 [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24816605; DOI=10.1128/jb.01716-14;
RA Lohsse A., Borg S., Raschdorf O., Kolinko I., Tompa E., Posfai M.,
RA Faivre D., Baumgartner J., Schueler D.;
RT "Genetic dissection of the mamAB and mms6 operons reveals a gene set
RT essential for magnetosome biogenesis in Magnetospirillum gryphiswaldense.";
RL J. Bacteriol. 196:2658-2669(2014).
CC -!- FUNCTION: Involved in redox-control of magnetite formation (By
CC similarity). 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 (By similarity). {ECO:0000250|UniProtKB:A0A1S7LCW6,
CC ECO:0000250|UniProtKB:Q2W8Q1}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:A0A1S7LCW6,
CC ECO:0000305|PubMed:23176475};
CC Note=Binds 2 heme groups via the magnetochrome (MCR) motifs.
CC {ECO:0000250|UniProtKB:A0A1S7LCW6, ECO:0000305|PubMed:23176475};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q2W8Q1}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q2W8Q1}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q2W8Q1}. Note=Not seen in magnetosome membranes.
CC {ECO:0000250|UniProtKB:Q2W8Q1}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
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:0000250|UniProtKB:Q2W8Q1}.
CC -!- DISRUPTION PHENOTYPE: Intermediate magnetic response, few large
CC magnetosomes with magnetite, makes many very small, irregular hematite
CC crystals. Near wild-type localization of MamC (PubMed:24816605).
CC Deletion of approximately 80 kb of DNA, including this operon, leads to
CC cells that are non-magnetic, lack internal membrane systems, grow
CC poorly, have reduced mobility and take-up and accumulate iron poorly
CC (PubMed:13129949). {ECO:0000269|PubMed:13129949,
CC ECO:0000269|PubMed:24816605}.
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 magnetosome MamP family. {ECO:0000305}.
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DR EMBL; AF374354; AAL09995.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12039.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30123.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78030.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99587.1; -; Genomic_DNA.
DR RefSeq; WP_024080583.1; NZ_CP027526.1.
DR AlphaFoldDB; Q93DZ0; -.
DR SMR; Q93DZ0; -.
DR STRING; 1430440.MGMSRv2_2372; -.
DR EnsemblBacteria; CDK99587; CDK99587; MGMSRv2__2372.
DR KEGG; mgry:MSR1_03430; -.
DR KEGG; mgy:MGMSRv2__2372; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_1029742_0_0_5; -.
DR OrthoDB; 884654at2; -.
DR Proteomes; UP000018922; Chromosome.
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; IPR036034; PDZ_sf.
DR Pfam; PF18509; MCR; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 3: Inferred from homology;
KW Biomineralization; Cell inner membrane; Cell membrane; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..270
FT /note="Multi-heme protein MamP"
FT /evidence="ECO:0000255"
FT /id="PRO_0000447782"
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..270
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 84..201
FT /note="PDZ"
FT /evidence="ECO:0000305|PubMed:24097349"
FT MOTIF 205..225
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:24097349"
FT MOTIF 245..269
FT /note="MCR 2"
FT /evidence="ECO:0000305|PubMed:24097349"
FT BINDING 219
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 222
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 223
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 263
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 266
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 267
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"
SQ SEQUENCE 270 AA; 28360 MW; F7C2D84E456017E5 CRC64;
MNSKLVLLVV GVVFALVLVI GRQGGVVAPQ SISVSPQMST AAPVAAPIAF PQATNVAMAV
EPMAAAGGTV AAMESPLPNF VPRNLKVFEG HWQGMDGRLM TEELARKLNY PRGVQGVLLG
EVTLNAAFSG LLGGDVVVRI DDTPVTNMEN FQAATRNVAN RSEARISVIR KDNRPGTPVL
RKLTVVLRAA EGGLGFAQLE GAPMILPGDP RPHGYRGACT DCHPVGQGFE LSPDPDLISL
PPSAITRDAV TRGVSPHEVR GPCEACHVIN
