MAMKL_MAGSA
ID MAMKL_MAGSA Reviewed; 339 AA.
AC P0DSO6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=MamK-like protein {ECO:0000303|PubMed:20161777};
DE EC=3.6.1.- {ECO:0000269|PubMed:24957623};
DE AltName: Full=Magnetosome cytoskeleton protein MamK-like {ECO:0000305};
GN Name=mamK-like {ECO:0000303|PubMed:20161777};
GN OrderedLocusNames=amb0397.1 {ECO:0000305};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
RN [2]
RP IDENTIFICATION, FUNCTION, EXPRESSION IN E.COLI, FORMS FILAMENTS,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20161777; DOI=10.1371/journal.pone.0009151;
RA Rioux J.B., Philippe N., Pereira S., Pignol D., Wu L.F., Ginet N.;
RT "A second actin-like MamK protein in Magnetospirillum magneticum AMB-1
RT encoded outside the genomic magnetosome island.";
RL PLoS ONE 5:E9151-E9151(2010).
RN [3]
RP FUNCTION, ATPASE ACTIVITY, FORMS FILAMENTS, BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH MAMK, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-15 AND ALA-141.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=24957623; DOI=10.1128/jb.01674-14;
RA Abreu N., Mannoubi S., Ozyamak E., Pignol D., Ginet N., Komeili A.;
RT "Interplay between two bacterial actin homologs, MamK and MamK-Like, is
RT required for the alignment of magnetosome organelles in Magnetospirillum
RT magneticum AMB-1.";
RL J. Bacteriol. 196:3111-3121(2014).
CC -!- FUNCTION: Protein with ATPase activity which forms pole-to-pole
CC filaments in vivo, probably with MamK. Efficient filament formation
CC requires MamK. Probably promotes turnover of MamK filaments, by
CC providing a monomer pool (PubMed:24957623). In vivo, in the absence of
CC its paralog MamK, forms thin filaments from pole to pole
CC (PubMed:20161777). In vitro forms straight filaments and bundles in the
CC absence of ATP. Filament formation is triggered by KCl and MgCl(2);
CC polymerizes more slowly and makes thinner filaments than MamK
CC (PubMed:20161777). Expression in E.coli yields a filament in the cell's
CC longitudinal axis; the protein nucleates at one pole or the cell septum
CC (PubMed:20161777). {ECO:0000269|PubMed:20161777,
CC ECO:0000269|PubMed:24957623}.
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:24957623};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=127 uM for ATP {ECO:0000269|PubMed:24957623};
CC -!- SUBUNIT: Forms cytoplasmic filament polymers (PubMed:20161777,
CC PubMed:24957623). Forms filaments with MamK (PubMed:24957623).
CC {ECO:0000269|PubMed:20161777, ECO:0000269|PubMed:24957623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20161777,
CC ECO:0000305|PubMed:24957623}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20161777, ECO:0000269|PubMed:24957623}.
CC Note=Protein forms filaments extending along most of the cell
CC associated with its inner curvature, in the correct position to be
CC filaments that are seen associated with magnetosomes (PubMed:20161777).
CC Colocalizes in filaments with paralog MamK (PubMed:24957623).
CC {ECO:0000269|PubMed:20161777, ECO:0000269|PubMed:24957623}.
CC -!- INDUCTION: Expressed during exponential phase in static growth
CC conditions in the presence and absence of the mamK gene
CC (PubMed:20161777). Expressed during late exponential phase in the
CC presence and absence of the mamK gene (PubMed:24957623).
CC {ECO:0000269|PubMed:20161777, ECO:0000269|PubMed:24957623}.
CC -!- DISRUPTION PHENOTYPE: About 40% reduction in magnetosome alignment; a
CC double mamK-mamK-like deletion has a 65% reduction in magnetosome
CC alignment. The single mamK-like deletion has no effect on MamK turnover
CC rates. {ECO:0000269|PubMed:24957623}.
CC -!- MISCELLANEOUS: This bacteria makes up to 20 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 -!- MISCELLANEOUS: Despite the presence of Ala-141 (where Glu is expected)
CC this protein has ATPase activity. {ECO:0000269|PubMed:24957623}.
CC -!- MISCELLANEOUS: Encoded in an approximately 22 kb magnetotaxis genomic
CC islet separate from the large magnetosome island.
CC {ECO:0000305|PubMed:20161777}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. MamK subfamily.
CC {ECO:0000305|PubMed:20161777}.
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; AP007255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DSO6; -.
DR SMR; P0DSO6; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0110148; P:biomineralization; IMP:UniProtKB.
DR InterPro; IPR043129; ATPase_NBD.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Biomineralization; Cytoplasm; Cytoskeleton; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..339
FT /note="MamK-like protein"
FT /id="PRO_0000447775"
FT BINDING 18..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 162..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT BINDING 216..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q6"
FT MUTAGEN 15
FT /note="D->N: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:24957623"
FT MUTAGEN 141
FT /note="A->E: Increased ATPase activity."
FT /evidence="ECO:0000269|PubMed:24957623"
SQ SEQUENCE 339 AA; 36953 MW; BD2F560421F19D33 CRC64;
MIVNDNQNIL YVGIDFGYSK TVIMTSRGKS LSLKSLVGYP KDFVGLARLG RPYLVGDEAF
EMRSYLHLRN PLLDGLLNPI SEQDIDVTRH FISHIIKCAE PAAGEKVFAV IGVTPRFTAA
NKKLLLKLAQ EYCQNVLLMS APFLAGNSIG KASGSIIIDI GAWTTDICAM KGRIPRPEDQ
SSIAKAGSYI DERLKNSILE RYPALQINAN IARMVKEQFA FVGRPQLVAA CEFRSAGKAV
RCDVTEQVRA ACESPFAEIA ERIGAVLCVV PPEDQALVLK NIVITGAGAQ IRGLPEYVKS
MLAPYGDARV SIANEPLMEA CKGALSMAQE IPPHFWGQL
