MAMY_MAGGM
ID MAMY_MAGGM Reviewed; 371 AA.
AC V6F5F3; Q3BK69;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Liposome tubulation protein MamY {ECO:0000305};
GN Name=mamY {ECO:0000303|PubMed:16237001}; OrderedLocusNames=MGMSRv2__2321;
GN ORFNames=mgI566, MGR_4150;
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP PROBABLE OPERON.
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 [7]
RP INDUCTION.
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 [8]
RP POSSIBLE FUNCTION, PROBABLE INTERACTION WITH MAMX AND MAMZ, SUBCELLULAR
RP 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: May be involved in constriction of the cell inner membrane to
CC form mature magnetosomes. Binds cardiolipin and liposomes (By
CC similarity). May function with MamX, MamZ amd Mms6 in biomineralization
CC (Probable). {ECO:0000250|UniProtKB:Q2W8K3,
CC ECO:0000305|PubMed:30367002}.
CC -!- SUBUNIT: Probably interacts with MamX and MamZ proteins.
CC {ECO:0000269|PubMed:30367002}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000305|PubMed:30367002}; Multi-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, rises to a maximum quickly (at
CC protein level) (PubMed:30367002). First gene in the 4 gene mamXY operon
CC (PubMed:20023033) (Probable). {ECO:0000269|PubMed:20023033,
CC ECO:0000269|PubMed:24020498, ECO:0000269|PubMed:30367002,
CC ECO:0000305|PubMed:22043287, ECO:0000305|PubMed:23889511,
CC ECO:0000305|PubMed:24020498}.
CC -!- DISRUPTION PHENOTYPE: Deletion of 4 consecutive genes (mamY, mamX,
CC mamZ, ftsZm) leads to cells with an intermediate magnetic response
CC where magnetosomes have short chains of nearly regularly shaped, cubo-
CC octahedral crystals flanked by small particles with poorly defined
CC morphologies. {ECO:0000269|PubMed:22043287}.
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 MamY family. {ECO:0000305}.
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DR EMBL; AM085146; CAJ30171.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78082.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99536.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F5F3; -.
DR STRING; 1430440.MGMSRv2_2321; -.
DR EnsemblBacteria; CDK99536; CDK99536; MGMSRv2__2321.
DR KEGG; mgry:MSR1_03880; -.
DR KEGG; mgy:MGMSRv2__2321; -.
DR HOGENOM; CLU_882247_0_0_5; -.
DR OrthoDB; 453796at2; -.
DR Proteomes; UP000018922; 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:0008289; F:lipid binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Biomineralization; Lipid-binding; Magnetosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..371
FT /note="Liposome tubulation protein MamY"
FT /id="PRO_0000447812"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..51
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 40896 MW; 4DB8BA147BE9BD72 CRC64;
MLMNFVNNVS KTINGGARIV YVGSFSWAVL SLLFVTAFSG WNNIFSMLPH EIFILVLTIS
LPIALIVLIF MLSQIVRTVE SVKSEISTLS QRDPVSEEAV TMLADLFREH RDAVAAQVAA
QVEATAQLVQ INQDNRALAA PSPDSGDENP LALLAQMFRE YRETVTAQLE AQISATTQLV
EASRDSRDGI VDELRSQRVL SQEITQELSH IAQSRNVVPV AEPGLDPSQR IDRMRALAEV
LGLALNDLSM TATQLLSEHL NAAHGDREGT QKFISTLTNA YFAGDKNVFF RSLVSEVVNH
SDQLQQCAIG AENVRQQISK ILREAREIRS LVSACDPNDL VRIVFEDGEL WALEKALAEH
FLIDGTPISD A
