ID   MAMX_MAGSA              Reviewed;         271 AA.
AC   Q2W8K4;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Magnetosome protein MamX {ECO:0000305};
DE   AltName: Full=Magnetochrome MamX {ECO:0000305};
GN   Name=mamX; OrderedLocusNames=amb1017;
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], AND SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Required for correct biomineralization of the magnetosome,
CC       may be involved in redox control of biomineralization. May function
CC       with MamY, MamZ amd Mms6. {ECO:0000250|UniProtKB:V6F2C2}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC       Note=Binds 2 heme groups per subunit via the 2 magnetochrome (MCR)
CC       motifs. {ECO:0000250|UniProtKB:V6F2C2};
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000269|PubMed:16303747}; Single-pass membrane protein
CC       {ECO:0000255}.
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   -!- SIMILARITY: Belongs to the magnetosome MamX family. {ECO:0000305}.
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DR   EMBL; AP007255; BAE49821.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W8K4; -.
DR   EnsemblBacteria; BAE49821; BAE49821; amb1017.
DR   KEGG; mag:amb1017; -.
DR   HOGENOM; CLU_942689_0_0_5; -.
DR   OMA; MVCSSCH; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0110146; C:magnetosome membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR040963; MCR.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   Pfam; PF18509; MCR; 2.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   3: Inferred from homology;
KW   Biomineralization; Heme; Iron; Magnetosome; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Magnetosome protein MamX"
FT                   /id="PRO_0000447788"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..271
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   MOTIF           48..71
FT                   /note="MCR (magnetochrome) 1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           87..110
FT                   /note="MCR 2"
FT                   /evidence="ECO:0000305"
FT   BINDING         65
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         68
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         69
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   BINDING         104
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000305"
FT   BINDING         107
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000305"
FT   BINDING         108
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"
SQ   SEQUENCE   271 AA;  28293 MW;  E12C65516F08DC8C CRC64;
     MSSKAVAHPN IAVWIMALGI AFSMALVLTA VFNANPWEDH TYDLAPPIVA GMPAPHRDGR
     EKMVCSSCHI VTPPAIGTGP GSGTLPIVQG TPAPHVDGRE KMPCASCHTI VKKGSVAKGA
     KAAPLPAAVT PGMPLPEAVS VALAVAPAPA AVPLGNEAHE RMVPFRYQGK VVSIAGAGAR
     SVWGDIYIQI NDGINPPIWI DLAPRWYLQA EGCVVRPGMF VKGTAFRDPT QAAAGLDYAM
     SVMANGEICA LRDNHLNGLW ANAGGMDAEE R