MAME_MAGGM
ID MAME_MAGGM Reviewed; 772 AA.
AC V6F2B6; Q6NE61;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Magnetosome formation protease MamE {ECO:0000305};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q2W8Q8};
DE AltName: Full=MM36.3 {ECO:0000303|PubMed:11571158};
DE AltName: Full=Magnetochrome MamE {ECO:0000303|PubMed:23176475};
DE AltName: Full=Magnetosome serine protease MamE {ECO:0000305};
GN Name=mamE {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2379;
GN ORFNames=mgI487, MGR_4091;
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], 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 [2]
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 [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 3-21, SUBCELLULAR LOCATION, AND POSSIBLE CLEAVAGE.
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 [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=14766587; DOI=10.1128/aem.70.2.1040-1050.2004;
RA Gruenberg K., Mueller E.C., Otto A., Reszka R., Linder D., Kube M.,
RA Reinhardt R., Schueler D.;
RT "Biochemical and proteomic analysis of the magnetosome membrane in
RT Magnetospirillum gryphiswaldense.";
RL Appl. Environ. Microbiol. 70:1040-1050(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=20674739; DOI=10.1016/j.resmic.2010.07.002;
RA Yang W., Li R., Peng T., Zhang Y., Jiang W., Li Y., Li J.;
RT "mamO and mamE genes are essential for magnetosome crystal
RT biomineralization in Magnetospirillum gryphiswaldense MSR-1.";
RL Res. Microbiol. 161:701-705(2010).
RN [8]
RP SUBUNIT.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=22007638; DOI=10.1111/j.1365-2958.2011.07863.x;
RA Uebe R., Junge K., Henn V., Poxleitner G., Katzmann E., Plitzko J.M.,
RA Zarivach R., Kasama T., Wanner G., Posfai M., Boettger L., Matzanke B.,
RA Schueler D.;
RT "The cation diffusion facilitator proteins MamB and MamM of
RT Magnetospirillum gryphiswaldense have distinct and complex functions, and
RT are involved in magnetite biomineralization and magnetosome membrane
RT assembly.";
RL Mol. Microbiol. 82:818-835(2011).
RN [9]
RP MINIMAL MAGNETOSOME ISLAND, PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
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 [10]
RP POSSIBLE COFACTOR, AND DOMAIN.
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 [11]
RP FUNCTION, AND MINIMAL VESICLE FORMATION GENES.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=27286560; DOI=10.1371/journal.pgen.1006101;
RA Raschdorf O., Forstner Y., Kolinko I., Uebe R., Plitzko J.M., Schueler D.;
RT "Genetic and Ultrastructural Analysis Reveals the Key Players and Initial
RT Steps of Bacterial Magnetosome Membrane Biogenesis.";
RL PLoS Genet. 12:E1006101-E1006101(2016).
CC -!- FUNCTION: Acts at 2 distinct steps of magnetosome formation; required
CC for correct localization of proteins to the magnetosome while the
CC protease activity is required for maturation of small magnetite
CC crystals into larger, functional ones (By similarity)
CC (PubMed:20674739). Probably cleaves at least itself, MamO and MamP;
CC cleavage requires the putative transprot domain of MamO (By
CC similarity). Involved in localization of some proteins (at least MamA,
CC MamC, MamF, MamI and MamJ) to the magnetosome (By similarity). One of 7
CC genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis;
CC coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon
CC restores magnetosome vesicle formation but not magnetite biosynthesis
CC (PubMed:27286560). {ECO:0000250|UniProtKB:Q2W8Q8,
CC ECO:0000269|PubMed:20674739, ECO:0000269|PubMed:27286560}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000305|PubMed:23176475};
CC Note=Probably binds 2-3 heme groups via the 3 magnetochrome (MCR)
CC motifs. {ECO:0000305, ECO:0000305|PubMed:23176475};
CC -!- SUBUNIT: Might interact with MamB via PDZ1.
CC {ECO:0000305|PubMed:22007638}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}; Single-pass
CC membrane protein {ECO:0000255}. Note=Purified magnetosomes remain
CC attached to each other. {ECO:0000269|PubMed:11571158}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- PTM: The protein isolated from magnetosome membranes has a molecular
CC weight of about 36.3 kDa, probably due to C-terminal cleavage
CC (PubMed:11571158). Subject to autocatalytic cleavage; cleavage also
CC requires MamO; these may be the same event (By similarity).
CC {ECO:0000250|UniProtKB:Q2W8Q8, ECO:0000269|PubMed:11571158}.
CC -!- DISRUPTION PHENOTYPE: Single gene deletion, loss of magnetic response,
CC about 35% iron content. Forms magnetosome chains without magnetosome
CC crystals (PubMed:20674739). Deletion of approximately 80 kb of DNA,
CC including this operon, leads to cells that are non-magnetic, lack
CC internal membrane systems, grow poorly, have reduced mobility and take-
CC up and accumulate iron poorly (PubMed:13129949).
CC {ECO:0000269|PubMed:13129949, ECO:0000269|PubMed:20674739}.
CC -!- MISCELLANEOUS: There is a third MCR motif in this protein (470-494)
CC that is not present in the M.magneticum strain AMB-1 MamE ortholog.
CC {ECO:0000305}.
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: In the N-terminal section; belongs to the peptidase S1C
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571797; CAE12032.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30116.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78023.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99594.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F2B6; -.
DR SMR; V6F2B6; -.
DR STRING; 1430440.MGMSRv2_2379; -.
DR EnsemblBacteria; CDK99594; CDK99594; MGMSRv2__2379.
DR KEGG; mgry:MSR1_03360; -.
DR KEGG; mgy:MGMSRv2__2379; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110146; C:magnetosome membrane; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR040963; MCR.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF18509; MCR; 3.
DR Pfam; PF17820; PDZ_6; 2.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF48695; SSF48695; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Biomineralization; Direct protein sequencing; Heme;
KW Hydrolase; Iron; Magnetosome; Membrane; Metal-binding; Protease;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..772
FT /note="Magnetosome formation protease MamE"
FT /id="PRO_0000447778"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..772
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 445..558
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 522..626
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 696..765
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT MOTIF 374..397
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:23176475"
FT MOTIF 420..443
FT /note="MCR 2"
FT /evidence="ECO:0000305"
FT MOTIF 470..494
FT /note="MCR 3"
FT /evidence="ECO:0000305|PubMed:23176475"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT BINDING 391
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305|PubMed:23176475"
FT BINDING 394
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305|PubMed:23176475"
FT BINDING 395
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:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305|PubMed:23176475"
FT BINDING 437
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305"
FT BINDING 440
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305"
FT BINDING 441
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:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305"
FT BINDING 488
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305|PubMed:23176475"
FT BINDING 491
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305|PubMed:23176475"
FT BINDING 492
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000305|PubMed:23176475"
FT CONFLICT 12
FT /note="G -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 78036 MW; 98DFE3DD488FBB8B CRC64;
MTMFNGDVED GGRSNVSCGK DLKRYLMLMG VVALVVLFGA FIYRQSSGGL RLGAMMEQMT
GARGAVNVPA QHGAPSAVVD PAMSVPARAR VAPPSAAGAI ATFPPVVDFG PAPVVSGGPF
TGVVTLLRNS VVSVTASSSG GQVMPDPLGL VNPDGLPRFA NPTTRSVENI GTGVIVRNDG
FIVTNYHVVR GANSVYVTVK DDVGSIRYSG EIVKMDEALD LALLKITPKV QLTAAVLGDS
DAVNVADEVI AIGTPFGLDM TVSRGIISAK RKTMVIEGMT HSNLLQTDAA INQGNSGGPL
VAANGTVVGI NTAIYTPNGA FAGIGFAVPS NQARLFALDE VGWLPTSTAE GPAMGLVAMQ
RPMGVGVGAA GPVIAAGTPS PHVDGRQNMD CSNCHDIIPA GNGFQAPMMP VAAPVPPPPI
PANAVSPHTD GRQNMTCNTC HQFVGGAAAG PIAFGQPMMP IAAPQQPAPA IRANAANPHT
DGRQNMNCAS CHQIIGSVGA APIAAPGAGG AYRFSQPPGS LAINIQGPRG GQGAVAGSGG
SRASLLGAAL TPLTQRLGLQ ANLPAGRGVF VNGVTPNTPA ASAGLRPGDV ILKVDGRPVH
QPEEVAAIMA EMPNGRSVRI GVLRAGDVSN MSLVTGPSGL AAAVVQAPTA PVVMAGGAPT
VPGVQPVIPK VPTEFNWLGM EIETFMAPQP VVGMPGATPV AGGGKGAQVA EVLAGSRAAV
AGLQANDLII EVNNRPVTSP ARLDAAIKAA TAAGQQILLK VHRNGQEFWI VL
