MAMT_MAGGM
ID MAMT_MAGGM Reviewed; 174 AA.
AC Q93DY4; Q6NE48; V6F5I9;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Magnetosome protein MamT {ECO:0000305};
DE AltName: Full=Magnetochrome MamT {ECO:0000303|PubMed:23176475};
GN Name=mamT {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2366;
GN ORFNames=mgI501, MGR_4104;
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 SUBCELLULAR LOCATION.
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 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 [8]
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 [9]
RP FUNCTION, AND 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: May play a role in magnetite crystal maturation (Probable).
CC May transfer electrons to balance the Fe(2+)-Fe(3+) ratio during
CC magnetite formation (Probable). {ECO:0000305|PubMed:23176475,
CC ECO:0000305|PubMed:24816605}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000305|PubMed:23176475};
CC Note=Probably binds 2 heme groups via the magnetochrome (MCR) motifs.
CC {ECO:0000305|PubMed:23176475};
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000305|PubMed:14766587}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- DISRUPTION PHENOTYPE: Normal magnetic response, slightly smaller,
CC irregularly spaced magnetosomes. Near wild-type localization of MamC
CC (PubMed:24816605). Deletion of approximately 80 kb of DNA, including
CC this operon, leads to cells that are non-magnetic, lack internal
CC membrane systems, grow poorly, have reduced mobility and take-up and
CC accumulate iron poorly (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 MamT family. {ECO:0000305}.
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DR EMBL; AF374354; AAL10001.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12045.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30129.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78036.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99581.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93DY4; -.
DR STRING; 1430440.MGMSRv2_2366; -.
DR EnsemblBacteria; CDK99581; CDK99581; MGMSRv2__2366.
DR KEGG; mgy:MGMSRv2__2366; -.
DR eggNOG; ENOG50346FK; Bacteria.
DR HOGENOM; CLU_1523388_0_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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR040963; MCR.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF18509; MCR; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
PE 3: Inferred from homology;
KW Biomineralization; Heme; Iron; Magnetosome; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..174
FT /note="Magnetosome protein MamT"
FT /id="PRO_0000447785"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..174
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 87..107
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:23176475"
FT MOTIF 138..158
FT /note="MCR 2"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 101
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 104
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 105
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:0000305|PubMed:23176475"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23176475"
FT BINDING 156
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:0000305|PubMed:23176475"
FT CONFLICT 30
FT /note="E -> K (in Ref. 1; AAL10001, 3; CAJ30129 and 4;
FT CAM78036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 18885 MW; 42A56718D32259CD CRC64;
MGTPGGGRRW MTLISITLLM VVGLGLYWDE LSLSAGISPA TSPRRAEGLL LGRLPLPMEP
SILSPLEHLI EPPLQYKLMT IRHIPPVMPG TGMPHPYVGD CIQCHLMVGG PAAGSQFKTP
YGAVLENLSR VRKLGPPILP TTRQPHPPAG RCIKCHDIVV KVPVEKKSGI KWLL
