MAMK_MAGGM
ID MAMK_MAGGM Reviewed; 360 AA.
AC Q6NE59; V6F2H8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Actin-like protein MamK {ECO:0000303|PubMed:20487281};
DE EC=3.6.1.- {ECO:0000269|PubMed:22586444};
DE AltName: Full=Magnetosome cytoskeleton protein MamK {ECO:0000305};
GN Name=mamK {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2377;
GN ORFNames=mgI489, MGR_4093;
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].
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 SUBUNIT, INTERACTION WITH MAMJ, AND SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION IN MAGNETOSOME SEGREGATION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=22026731; DOI=10.1111/j.1365-2958.2011.07874.x;
RA Katzmann E., Mueller F.D., Lang C., Messerer M., Winklhofer M.,
RA Plitzko J.M., Schueler D.;
RT "Magnetosome chains are recruited to cellular division sites and split by
RT asymmetric septation.";
RL Mol. Microbiol. 82:1316-1329(2011).
RN [8]
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 [9]
RP FUNCTION, ATPASE ACTIVITY, FORMS FILAMENTS, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=22586444; DOI=10.1371/journal.pone.0034189;
RA Sonkaria S., Fuentes G., Verma C., Narang R., Khare V., Fischer A.,
RA Faivre D.;
RT "Insight into the assembly properties and functional organisation of the
RT magnetotactic bacterial actin-like homolog, MamK.";
RL PLoS ONE 7:E34189-E34189(2012).
RN [10]
RP FORMS FILAMENTS, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24272781; DOI=10.1128/jb.00804-13;
RA Mueller F.D., Raschdorf O., Nudelman H., Messerer M., Katzmann E.,
RA Plitzko J.M., Zarivach R., Schueler D.;
RT "The FtsZ-like protein FtsZm of Magnetospirillum gryphiswaldense likely
RT interacts with its generic homolog and is required for biomineralization
RT under nitrate deprivation.";
RL J. Bacteriol. 196:650-659(2014).
RN [11]
RP FUNCTION IN MAGNETOSOME SEGREGATION, ACTIVITY REGULATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-174.
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: Protein with ATPase activity which forms dynamic cytoplasmic
CC filaments that are involved in sorting, concatenating and/or correctly
CC positioning of magnetosomes in the cell. Not absolutely necessary for
CC assembly of short chains (PubMed:20487281, PubMed:22586444,
CC PubMed:27733152). Filaments grow from the both cell poles towards
CC midcell, and are probably disassembled at the other end of the cell, a
CC process known as treadmilling (PubMed:27733152). Polymerizes in the
CC presence of ATP, GTP or a non-hydrolyzable ATP analog
CC (PubMed:22586444). Required for correct segregation and positioning of
CC magnetosomes following cell division (PubMed:22026731,
CC PubMed:27733152). {ECO:0000269|PubMed:20487281,
CC ECO:0000269|PubMed:22026731, ECO:0000269|PubMed:22586444,
CC ECO:0000269|PubMed:27733152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22586444};
CC -!- ACTIVITY REGULATION: Filament dynamics depend partially on MamJ.
CC {ECO:0000269|PubMed:27733152}.
CC -!- SUBUNIT: Forms cytoplasmic filaments (PubMed:17601786, PubMed:20487281,
CC PubMed:22026731, PubMed:22586444, PubMed:24272781). Interacts with MamJ
CC (PubMed:17601786). Forms filaments in the absence of other magnetosome
CC proteins and in E.coli (PubMed:20487281). Filament formation in vitro
CC requires ATP, GTP or a non-hydrolyzable ATP analog (PubMed:22586444).
CC {ECO:0000269|PubMed:17601786, ECO:0000269|PubMed:20487281,
CC ECO:0000269|PubMed:22026731, ECO:0000269|PubMed:22586444,
CC ECO:0000269|PubMed:24272781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17601786,
CC ECO:0000305|PubMed:20487281, ECO:0000305|PubMed:22026731,
CC ECO:0000305|PubMed:22586444, ECO:0000305|PubMed:24272781}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:17601786,
CC ECO:0000269|PubMed:20487281}. Note=Tagged protein forms straight lines
CC extending along most of the cell associated with its inner curvature,
CC in the correct position to be filaments that are seen associated with
CC magnetosomes (PubMed:17601786, PubMed:20487281). The exact pattern
CC depends on the N- or C-terminal location of the tag and the length of
CC the linker to the rest of the protein (PubMed:20487281). Individual
CC filaments are 3-6 nm in diameter and 0.5-1 nm in length and
CC occasionally form bundles. Filaments are in close proximity to
CC magnetosome membranes. Most are near midcell, however some extend to
CC nearly the cell pole; they are not seen in a deletion mutant
CC (PubMed:20487281). Filaments do not colocalize with FtsZ-like (also
CC called FtsZm) foci (PubMed:24272781). {ECO:0000269|PubMed:17601786,
CC ECO:0000269|PubMed:20487281, ECO:0000269|PubMed:24272781}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949, ECO:0000305|PubMed:22043287}.
CC -!- DISRUPTION PHENOTYPE: Non-polar single gene deletion has wild-type
CC growth and motility. Has half the number of magnetosomes which are
CC mostly incorrectly positioned and of lower chain length; magnetite
CC crystals and magnetosome morphology are normal. No magnetosome-
CC associated filaments are seen (PubMed:20487281, PubMed:27733152).
CC Incorrect subcellular location of MamJ (PubMed:20487281). Incorrect
CC positioning of magnetosomes in dividing cells, leads to uneven
CC distribution of magnetosome crystals (PubMed:22026731,
CC PubMed:27733152). Deletion of 3 consecutive genes (mamJ, mamK, mamL)
CC leads to cells devoid of magnetosomes or a magnetic response
CC (PubMed:22043287). Deletion of approximately 80 kb of DNA, including
CC this operon, leads to cells that are non-magnetic, lack internal
CC membrane systems, grow poorly, have reduced mobility and take-up and
CC accumulate iron poorly (PubMed:13129949). {ECO:0000269|PubMed:13129949,
CC ECO:0000269|PubMed:20487281, ECO:0000269|PubMed:22026731,
CC ECO:0000269|PubMed:22043287, ECO:0000269|PubMed:27733152}.
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 -!- MISCELLANEOUS: In the related bacteria M.magneticum strain AMB the
CC magnetosome position remains stable during cytokinesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. MamK subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDK99592.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX571797; CAE12034.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30118.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78025.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99592.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6NE59; -.
DR SMR; Q6NE59; -.
DR STRING; 1430440.MGMSRv2_2377; -.
DR EnsemblBacteria; CDK99592; CDK99592; MGMSRv2__2377.
DR KEGG; mgy:MGMSRv2__2377; -.
DR eggNOG; COG1077; Bacteria.
DR HOGENOM; CLU_052037_3_0_5; -.
DR OrthoDB; 410781at2; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0110148; P:biomineralization; IMP:UniProtKB.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Biomineralization; Cytoplasm; Cytoskeleton; GTP-binding;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..360
FT /note="Actin-like protein MamK"
FT /id="PRO_0000447773"
FT BINDING 22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 33..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 177..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 231..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT MUTAGEN 174
FT /note="D->A: Magnetosome chain partitioning, movement and
FT placement in cell is seriously impaired, many cells have
FT fragmented chains. Impaired magnetic response. Has lost
FT MamK dynamics, probably has no ATPase activity. Cells do
FT not separate totally. No effect on MamJ movement.
FT Magnetosome missegregation in offspring."
FT /evidence="ECO:0000269|PubMed:27733152"
FT CONFLICT 1..13
FT /note="Missing (in Ref. 4; CDK99592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39199 MW; A751CBB4C0BA9E29 CRC64;
MWIDLLARER SDKMSEGEGQ AKNRLFLGID LGTSHTAVMT SRGKKFLLKS VVGYPKDVIG
LKLLGRPYVV GDEAFEMRSY LDLRYPLQDG VLSEISDRDI EVARHLLTHV VKSAEPGAND
EICAVIGVPA RASGANKALL LKMAQEVVHT ALVVSEPFMV GYGLDKLNNT IIVDIGAGTT
DICALKGTVP GPEDQVTLTK AGNYLDERLQ NAILERHPEL QMNTNVACAV KEQFSFVGAR
GEAATFEFRA AGKPVRCDVT ESVKIACEAL MPDIIESIEI LLRSFQPEYQ ATVLQNIVFA
GGGSRIRGLA AYVKDKLRPF GNADVTCVKD PTFDGCRGAL RLAEELPPQY WCQLGDVSGQ
