ID   LIMJ_MAGSA              Reviewed;         319 AA.
AC   Q2W8L8;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=MamJ paralog LimJ {ECO:0000303|PubMed:21883528};
GN   Name=limJ {ECO:0000303|PubMed:21883528}; OrderedLocusNames=amb1003;
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], AND SUBCELLULAR LOCATION.
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=21883528; DOI=10.1111/j.1365-2958.2011.07815.x;
RA   Draper O., Byrne M.E., Li Z., Keyhani S., Barrozo J.C., Jensen G.,
RA   Komeili A.;
RT   "MamK, a bacterial actin, forms dynamic filaments in vivo that are
RT   regulated by the acidic proteins MamJ and LimJ.";
RL   Mol. Microbiol. 82:342-354(2011).
CC   -!- FUNCTION: Regulates the dynamic behavior of MamK filaments; paralog
CC       MamJ also promotes MamK turnover. At least one other protein besides
CC       MamJ and LimJ is required for MamK turnover (PubMed:21883528). Might
CC       connect magnetosomes to MamK filaments (Probable).
CC       {ECO:0000269|PubMed:21883528, ECO:0000305|PubMed:21883528}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome {ECO:0000269|PubMed:16303747,
CC       ECO:0000305|PubMed:21883528}. Note=Tagged protein extends in a line
CC       from one pole to the other. {ECO:0000250|UniProtKB:Q2W8Q7,
CC       ECO:0000305|PubMed:21883528}.
CC   -!- DOMAIN: The center of the protein is Glu- and Pro-rich. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Single gene deletion, no effect on magnetic
CC       response, the magnetosome chain or MamK filaments. A double mamJ/limJ
CC       deletion has wild-type magnetic response, but forms large gaps in the
CC       magnetosome chains reminiscent of the mamK deletion. MamK forms bundles
CC       in these gaps, but the MamK filaments are no longer dynamic.
CC       {ECO:0000269|PubMed:21883528}.
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   -!- SIMILARITY: Belongs to the magnetosome MamJ protein family.
CC       {ECO:0000305}.
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DR   EMBL; AP007255; BAE49807.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W8L8; -.
DR   EnsemblBacteria; BAE49807; BAE49807; amb1003.
DR   KEGG; mag:amb1003; -.
DR   HOGENOM; CLU_870976_0_0_5; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0110143; C:magnetosome; IMP:UniProtKB.
DR   GO; GO:0110148; P:biomineralization; IMP:UniProtKB.
PE   3: Inferred from homology;
KW   Biomineralization; Magnetosome; Reference proteome.
FT   CHAIN           1..319
FT                   /note="MamJ paralog LimJ"
FT                   /id="PRO_0000447805"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  32873 MW;  74F2BD4F279D5149 CRC64;
     MMMEHEMATN RRPRAKRTPG DKLGKGGGDA ALAPAADAEI PASSAPEPAA PISAPPAPVI
     KPVGGDAWAS LLSGSPWSSP GAASPTEAAL KPVMPSALAE AVANAPPEAA PFTELVSHWS
     PPFRRQPDRE YEEINPAEAA IPVTAAAPEP EPEPVPEPEP EPEPEAAHDH AATETEGVTE
     MMTSDVELEI EIASDVEVVE APAVIEPSPR PQAFSHSTAY AYPAEPAPAV ETAAEAAPAG
     PAENPVKEVP VEDLFTGIFN VADSAVRGAI GASTDLLRDP KSLGGKLSVA GQSLVHSIKG
     RFNALLAPRH GAKSNGDEF