MAMJ_MAGGM
ID MAMJ_MAGGM Reviewed; 466 AA.
AC V6F519; Q3BKB2; Q6NE60;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Magnetosome-associated protein MamJ {ECO:0000305};
GN Name=mamJ {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2378;
GN ORFNames=mgI488, MGR_4092;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 251.
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 [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-10, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=16299495; DOI=10.1038/nature04382;
RA Scheffel A., Gruska M., Faivre D., Linaroudis A., Plitzko J.M.,
RA Schueler D.;
RT "An acidic protein aligns magnetosomes along a filamentous structure in
RT magnetotactic bacteria.";
RL Nature 440:110-114(2006).
RN [7]
RP SUBUNIT, INTERACTION WITH MAMK, DISRUPTION PHENOTYPE, AND VARIANT
RP 252-GLU--ALA-291 DEL.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=17601786; DOI=10.1128/jb.00421-07;
RA Scheffel A., Schueler D.;
RT "The acidic repetitive domain of the Magnetospirillum gryphiswaldense MamJ
RT protein displays hypervariability but is not required for magnetosome chain
RT assembly.";
RL J. Bacteriol. 189:6437-6446(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=20487281; DOI=10.1111/j.1365-2958.2010.07202.x;
RA Katzmann E., Scheffel A., Gruska M., Plitzko J.M., Schueler D.;
RT "Loss of the actin-like protein MamK has pleiotropic effects on magnetosome
RT formation and chain assembly in Magnetospirillum gryphiswaldense.";
RL Mol. Microbiol. 77:208-224(2010).
RN [9]
RP MINIMAL MAGNETOSOME ISLAND, 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 [10]
RP FUNCTION IN MAGNETOSOME SEGREGATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=27733152; DOI=10.1186/s12915-016-0290-1;
RA Toro-Nahuelpan M., Mueller F.D., Klumpp S., Plitzko J.M., Bramkamp M.,
RA Schueler D.;
RT "Segregation of prokaryotic magnetosomes organelles is driven by
RT treadmilling of a dynamic actin-like MamK filament.";
RL BMC Biol. 14:88-88(2016).
CC -!- FUNCTION: Required for assembly of magnetosome chains
CC (PubMed:16299495). Regulates the dynamic behavior of MamK filaments (By
CC similarity). May connect magnetosomes to MamK filaments (Probable).
CC Moves from the cell poles towards midcell; movement does not depend on
CC the treadmilling ability of MamK, suggesting MamJ associates and
CC disassociates continuously from the MamK filament (PubMed:27733152).
CC {ECO:0000250|UniProtKB:Q2W8Q7, ECO:0000269|PubMed:16299495,
CC ECO:0000269|PubMed:27733152, ECO:0000305|PubMed:16299495,
CC ECO:0000305|PubMed:17601786, ECO:0000305|PubMed:27733152}.
CC -!- SUBUNIT: Forms homooligomers (Probable) (PubMed:17601786). Interacts
CC with MamK (PubMed:17601786). {ECO:0000269|PubMed:17601786,
CC ECO:0000305|PubMed:14766587}.
CC -!- SUBCELLULAR LOCATION: Magnetosome {ECO:0000269|PubMed:14766587}.
CC Note=Tagged protein extends from one pole to the other, and is longer
CC than the magnetosome chain (PubMed:16299495). Correct subcellular
CC location requires MamK (PubMed:20487281). {ECO:0000269|PubMed:16299495,
CC ECO:0000269|PubMed:20487281}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949, ECO:0000305|PubMed:22043287}.
CC -!- DOMAIN: The gene is quite polymorphic, the central region is subject to
CC recombination between internal Glu-Pro-rich repeats (Probable). The
CC polymorphic central region is not required for function, small segments
CC in the N- and C-terminus are however required (PubMed:17601786).
CC {ECO:0000269|PubMed:17601786, ECO:0000305|PubMed:17601786}.
CC -!- PTM: Identified by N-terminal sequencing of a protein that is about 96
CC kDa in size (PubMed:14766587). The protein runs anomalously on protein
CC gels (PubMed:17601786). {ECO:0000269|PubMed:14766587,
CC ECO:0000269|PubMed:17601786}.
CC -!- DISRUPTION PHENOTYPE: Single gene deletion has compact clusters of
CC magnetosomes instead of magnetosome chains; precursor magnetosome
CC vesicles and vesicles containing immature crystals are throughout the
CC cytoplasm and no longer associated with filaments. Cells have
CC substantially decreased magnetic orientation (PubMed:16299495,
CC PubMed:17601786). No change in location of MamK (PubMed:17601786).
CC Single deletion slows recovery of MamK dynamics following
CC photobleaching (PubMed:27733152). Deletion of 3 consecutive genes
CC (mamJ, mamK, mamL) leads to cells devoid of magnetosomes or a magnetic
CC response (PubMed:22043287). Deletion of approximately 80 kb of DNA,
CC including this operon, leads to cells that are non-magnetic, lack
CC internal membrane systems, grow poorly, have reduced mobility and take-
CC up and accumulate iron poorly (PubMed:13129949).
CC {ECO:0000269|PubMed:13129949, ECO:0000269|PubMed:16299495,
CC ECO:0000269|PubMed:17601786, ECO:0000269|PubMed:22043287,
CC ECO:0000269|PubMed:27733152}.
CC -!- MISCELLANEOUS: The gene is quite polymorphic, the central region is
CC subject to recombination between similar Glu- and Pro-rich repeats.
CC {ECO:0000305|PubMed:17601786}.
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:13129949}.
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 MamJ protein family.
CC {ECO:0000305}.
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DR EMBL; BX571797; CAE12033.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30117.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78024.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99593.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F519; -.
DR STRING; 1430440.MGMSRv2_2378; -.
DR EnsemblBacteria; CDK99593; CDK99593; MGMSRv2__2378.
DR KEGG; mgy:MGMSRv2__2378; -.
DR HOGENOM; CLU_538390_0_0_5; -.
DR OrthoDB; 1426014at2; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0110143; C:magnetosome; IDA:UniProtKB.
DR GO; GO:0110148; P:biomineralization; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Biomineralization; Direct protein sequencing; Magnetosome;
KW Reference proteome; Repeat.
FT CHAIN 1..466
FT /note="Magnetosome-associated protein MamJ"
FT /id="PRO_0000447803"
FT REPEAT 81..168
FT /note="Tandem repeat unit 1"
FT /evidence="ECO:0000269|PubMed:16299495"
FT REPEAT 145..164
FT /note="Glu-Pro-rich motif 1"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REPEAT 169..256
FT /note="Tandem repeat unit 2"
FT /evidence="ECO:0000269|PubMed:16299495"
FT REPEAT 233..252
FT /note="Glu-Pro-rich motif 2"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REPEAT 253..272
FT /note="Glu-Pro-rich motif 3"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 1..24
FT /note="Not required to restore magnetic response to
FT deletion mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..80
FT /note="Required to restore magnetic response to deletion
FT mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..256
FT /note="Not required to restore magnetic response to
FT deletion mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 136..334
FT /note="Not required to restore magnetic response to
FT deletion mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 333..374
FT /note="Not required to restore magnetic response to
FT deletion mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 375..432
FT /note="Required to restore magnetic response to deletion
FT mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 426..466
FT /note="Required to restore magnetic response to deletion
FT mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT REGION 432..466
FT /note="Not required to restore magnetic response to
FT deletion mutant"
FT /evidence="ECO:0000269|PubMed:17601786"
FT COMPBIAS 60..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 252..291
FT /note="Missing (in variant 252-Glu--Ala-291 del)"
SQ SEQUENCE 466 AA; 48517 MW; 049686E7B53F938D CRC64;
MAKNRRDRGT DLPGDGDQKI STGPEIVSVT VHPSPNLAAA AKPVQGDIWA SLLESSPWSA
NQGGLVETAQ PPSAPIRSQD PVPVADLVNR WSQPIWRTAP LAGNAESSEE GVVAPSLTQS
DSVLAVSDLV IDVQPETDAE VEVSIEPEPA LVEPVIEIEA EAAEVEPEPA PVADLVNRWA
QPIWRTAPLA GNAESSEEGV VAPSLTQSDS VLAVSDLVID VQPEANAEVE VSIEPEPALV
EPVIEIEAEA AEVEPEPAPV EPVIEIEAEA AEVEPEPAPV EPVIEIEAEA AEVEPEPAPV
EPAIEIEAIR VELEPVLIDE VVELVTEFEY SQAESVASAD LIANPAPAES SRLAELLDEA
AAIAAPAVAV AVEATRQPNK ITASVKKRAP VQEVPVEDLL GGIFGVAGSA VRGVFTIGGG
FVDGVVKGGR LVGSNVVAGT RRLAQTIEVS CGSCSSPKCD AEDKNK
