MAMX_MAGGM
ID MAMX_MAGGM Reviewed; 269 AA.
AC V6F2C2; A4U5C4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Magnetosome protein MamX {ECO:0000305};
DE AltName: Full=Magnetochrome MamX {ECO:0000303|PubMed:23889511};
GN Name=mamX {ECO:0000303|PubMed:17449609}; OrderedLocusNames=MGMSRv2__2322;
GN ORFNames=MGR_4149;
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 [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 [2]
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 [3]
RP INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=20023033; DOI=10.1128/jb.01292-09;
RA Ding Y., Li J., Liu J., Yang J., Jiang W., Tian J., Li Y., Pan Y., Li J.;
RT "Deletion of the ftsZ-like gene results in the production of
RT superparamagnetic magnetite magnetosomes in Magnetospirillum
RT gryphiswaldense.";
RL J. Bacteriol. 192:1097-1105(2010).
RN [4]
RP 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 [5]
RP FUNCTION, POSSIBLE COFACTOR, PROBABLE OPERON, DOMAIN, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 65-CYS--CYS-68 AND 104-CYS--CYS-107.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=23889511; DOI=10.1111/mmi.12317;
RA Raschdorf O., Mueller F.D., Posfai M., Plitzko J.M., Schueler D.;
RT "The magnetosome proteins MamX, MamZ and MamH are involved in redox control
RT of magnetite biomineralization in Magnetospirillum gryphiswaldense.";
RL Mol. Microbiol. 89:872-886(2013).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24020498; DOI=10.1186/1471-2180-13-203;
RA Yang J., Li S., Huang X., Li J., Li L., Pan Y., Li Y.;
RT "MamX encoded by the mamXY operon is involved in control of magnetosome
RT maturation in Magnetospirillum gryphiswaldense MSR-1.";
RL BMC Microbiol. 13:203-203(2013).
RN [7]
RP POSSIBLE FUNCTION, PROBABLE INTERACTION WITH FTSZ-LIKE AND MAMY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=30367002; DOI=10.1128/aem.02394-18;
RA Wang Q., Wu S., Li X., Zhang T., Yang J., Wang X., Li F., Li Y., Peng Y.,
RA Li J.;
RT "Work Patterns of MamXY Proteins during Magnetosome Formation in
RT Magnetospirillum gryphiswaldense MSR-1.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
CC -!- FUNCTION: Required for correct biomineralization of the magnetosome,
CC maybe via redox control (PubMed:23889511, PubMed:24020498). May
CC function with MamY, MamZ amd Mms6 in biomineralization (Probable).
CC {ECO:0000269|PubMed:23889511, ECO:0000269|PubMed:24020498,
CC ECO:0000305|PubMed:30367002}.
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:0000305|PubMed:23889511};
CC -!- SUBUNIT: Probably interacts with FtsZ-like and MamY proteins.
CC {ECO:0000269|PubMed:30367002}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000305|PubMed:30367002}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expressed in exponential phase, peaks about 18 hours
CC (PubMed:20023033, PubMed:24020498). Protein is associated with
CC magnetosomes as they start to develop, maximal protein is detected
CC early then decreases (at protein level) (PubMed:30367002). Second gene
CC in the 4 gene mamXY operon (PubMed:20023033) (Probable).
CC {ECO:0000269|PubMed:20023033, ECO:0000269|PubMed:24020498,
CC ECO:0000269|PubMed:30367002, ECO:0000305|PubMed:22043287,
CC ECO:0000305|PubMed:23889511, ECO:0000305|PubMed:24020498}.
CC -!- DOMAIN: The C-terminus of the protein cannot be tagged, suggesting it
CC is required for function. {ECO:0000269|PubMed:23889511}.
CC -!- DISRUPTION PHENOTYPE: Slightly reduced magnetic response, produces
CC chains of wild-type magnetite crystals sandwiched between irregularly
CC shaped, small flake-like crystals. Small crystals are in magnetosomes,
CC but some have multiple nucleation sites. Phenotype is exacerbated when
CC grown in NH(4)(+) instead of NO(3)(-) medium. Deletion of the
CC periplasmic nitrate reductase operon also exacerbates the phenotype.
CC Deletion mutants probably make some hematite crystals as well as wild-
CC type magnetite crystals (PubMed:23889511). Loss of magnetic response,
CC considerable decrease in intracellular iron. Magnetosomes are normally
CC organized but the crystals are irregular, smaller superparamagnetic
CC magnetite particles. Increased expression of the downstream genes in
CC the operon (mamZ and ftsZ-like) (PubMed:24020498). Deletion of 4
CC consecutive genes (mamY, mamX, mamZ, ftsZm) leads to cells with an
CC intermediate magnetic response where magnetosomes have short chains of
CC nearly regularly shaped, cubo-octahedral crystals flanked by small
CC particles with poorly defined morphologies (PubMed:22043287).
CC {ECO:0000269|PubMed:22043287, ECO:0000269|PubMed:23889511,
CC ECO:0000269|PubMed:24020498}.
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}.
CC -!- SIMILARITY: Belongs to the magnetosome MamX family. {ECO:0000305}.
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DR EMBL; CU459003; CAM78081.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99537.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F2C2; -.
DR STRING; 1430440.MGMSRv2_2322; -.
DR EnsemblBacteria; CDK99537; CDK99537; MGMSRv2__2322.
DR KEGG; mgy:MGMSRv2__2322; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_942689_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; IMP: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 1: Evidence at protein level;
KW Biomineralization; Heme; Iron; Magnetosome; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Magnetosome protein MamX"
FT /id="PRO_0000447787"
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..269
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 48..71
FT /note="MCR (magnetochrome) 1"
FT /evidence="ECO:0000305|PubMed:23889511"
FT MOTIF 87..110
FT /note="MCR 2"
FT /evidence="ECO:0000305|PubMed:23889511"
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 ECO:0000305|PubMed:23889511"
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 ECO:0000305|PubMed:23889511"
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 ECO:0000305|PubMed:23889511"
FT BINDING 104
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23889511"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:23889511"
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|PubMed:23889511"
FT MUTAGEN 65..68
FT /note="CSSC->ASSA: Phenocopies deletion mutant; reduced
FT magnetic response, makes regular crystals sandwiched
FT between flake-like crystals; when associated with A-104--
FT 107-A."
FT /evidence="ECO:0000269|PubMed:23889511"
FT MUTAGEN 104..107
FT /note="CASC->AASA: Phenocopies deletion mutant; reduced
FT magnetic response, makes regular crystals sandwiched
FT between flake-like crystals; when associated with A-65--68-
FT A."
FT /evidence="ECO:0000269|PubMed:23889511"
SQ SEQUENCE 269 AA; 28221 MW; C544B4034545E064 CRC64;
MNTKAVAHPD IAVWIMALGI AFSMALVLTA LFNANPWEDH TYDLAPPIVA GMAAPHRDGR
EKMVCSSCHI VTPASAATGP GAGTLPIVEG TPAPHVDGRE KMACASCHTI VKKGSVAKSG
KASPAPVAFS QGMPLPEAMS VALAVTPAPA PLGNEAHERM VPFRYQGKIV SVAGAGTRSV
WGDIYIQIND GINPPMWIDL APLWFLQAEG CLVRPGMFVK GTAFRDPTQA SAGLDYAMSV
MANGEVCALR DDHLNGLWAN VGGVDAEER
