MAMC_MAGMM
ID MAMC_MAGMM Reviewed; 133 AA.
AC A0L9X3;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Magnetosome protein MamC {ECO:0000305};
GN Name=mamC {ECO:0000303|PubMed:24760293}; OrderedLocusNames=Mmc1_2265;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=24760293; DOI=10.1007/s00203-014-0984-0;
RA Valverde-Tercedor C., Abadia-Molina F., Martinez-Bueno M.,
RA Pineda-Molina E., Chen L., Oestreicher Z., Lower B.H., Lower S.K.,
RA Bazylinski D.A., Jimenez-Lopez C.;
RT "Subcellular localization of the magnetosome protein MamC in the marine
RT magnetotactic bacterium Magnetococcus marinus strain MC-1 using
RT immunoelectron microscopy.";
RL Arch. Microbiol. 196:481-488(2014).
RN [3]
RP SELF-ASSEMBLY.
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX DOI=10.1155/2014/320124;
RA Kashyap S., Woeh T., Valverde-Tercedor C., Sanchez-Quesada M.,
RA Jimenez Lopez C., Prozorov T.;
RT "Visualization of iron-binding micelles in acidic recombinant
RT biomineralization protein, MamC.";
RL (er) J. Nanomater. 320124 (2014).
RN [4]
RP FUNCTION, IRON-BINDING, AND POSSIBLE TOPOLOGY.
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=25874532; DOI=10.1007/s00253-014-6326-y;
RA Valverde-Tercedor C., Montalban-Lopez M., Perez-Gonzalez T.,
RA Sanchez-Quesada M.S., Prozorov T., Pineda-Molina E., Fernandez-Vivas M.A.,
RA Rodriguez-Navarro A.B., Trubitsyn D., Bazylinski D.A., Jimenez-Lopez C.;
RT "Size control of in vitro synthesized magnetite crystals by the MamC
RT protein of Magnetococcus marinus strain MC-1.";
RL Appl. Microbiol. Biotechnol. 99:5109-5121(2015).
RN [5]
RP FUNCTION, DOMAIN, AND IRON-BINDING.
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=26970040; DOI=10.1016/j.jsb.2016.03.001;
RA Nudelman H., Tercedor C.V., Kolusheva S., Gonzalez T.P., Widdrat M.,
RA Grimberg N., Levi H., Nelkenbaum O., Davidov G., Faivre D.,
RA Jimenez-Lopez C., Zarivach R.;
RT "Structure-function studies of the magnetite-biomineralizing magnetosome-
RT associated protein MamC.";
RL J. Struct. Biol. 194:244-252(2016).
CC -!- FUNCTION: Probably helps control the size of magnetite crystals; in
CC vitro synthesis of magnetite yields larger and more well-developed
CC magnetite crystals in the presence of purified MamC (PubMed:25874532,
CC PubMed:26970040). Binds Fe(3+) (PubMed:25874532). The lumenal domain
CC probably binds magnetite crystals, affecting crystal size and shape
CC (Probable). Purified MamC self-assembles into micelles in the presence
CC of ferric chloride hexahydrate (FeCl(3).6H(2)O); both oxygen and iron
CC are present in the proteinaceous micelles. Whether this is relevant in
CC vivo is unknown (Ref.3). {ECO:0000269|PubMed:25874532,
CC ECO:0000269|PubMed:26970040, ECO:0000269|Ref.3,
CC ECO:0000305|PubMed:26970040}.
CC -!- SUBUNIT: Probably interacts with MamA. {ECO:0000250|UniProtKB:Q93DY1}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:24760293}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The lumenal magnetite interacting component (MIC, residues 37-
CC 57) probably binds magnetite. {ECO:0000250|UniProtKB:Q2W8S0,
CC ECO:0000305|PubMed:26970040}.
CC -!- MISCELLANEOUS: This bacteria makes magnetosomes having a pseudo-
CC hexagonal prismatic crystal of magnetite (Fe(3)O(4)).
CC {ECO:0000305|PubMed:24760293}.
CC -!- SIMILARITY: Belongs to the magnetosome MamC 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; CP000471; ABK44766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0L9X3; -.
DR EnsemblBacteria; ABK44766; ABK44766; Mmc1_2265.
DR KEGG; mgm:Mmc1_2265; -.
DR eggNOG; ENOG5033G8Q; Bacteria.
DR HOGENOM; CLU_1989955_0_0_5; -.
DR OMA; NAMSGAC; -.
DR OrthoDB; 2203920at2; -.
DR Proteomes; UP000002586; 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.
PE 1: Evidence at protein level;
KW Biomineralization; Iron; Magnetosome; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..133
FT /note="Magnetosome protein MamC"
FT /id="PRO_0000447791"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..67
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:25874532"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 37..57
FT /note="Magnetite interacting component (MIC) binds
FT magnetite"
FT /evidence="ECO:0000250|UniProtKB:Q2W8S0,
FT ECO:0000305|PubMed:26970040"
FT REGION 105..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 133 AA; 13601 MW; 799662F157ADDF9D CRC64;
MAAFNLALYL SKSIPGVGVL GGVIGGSAAL AKNLKAKQRG EITTEEAVID TGKEALGAGL
ATTVSAYAAG VVGGGLVVSL GTAFAVAVAG KYAWDYGMEQ MEAKLQEKKH QEQGGQTYGD
NPDPFDPQEL ETP
