MAMU_MAGGM
ID MAMU_MAGGM Reviewed; 297 AA.
AC Q6NE47; V6F225;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Putative lipid kinase MamU {ECO:0000305};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00783};
GN Name=mamU {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2365;
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 [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 [3]
RP MINIMAL MAGNETOSOME ISLAND.
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 [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24816605; DOI=10.1128/jb.01716-14;
RA Lohsse A., Borg S., Raschdorf O., Kolinko I., Tompa E., Posfai M.,
RA Faivre D., Baumgartner J., Schueler D.;
RT "Genetic dissection of the mamAB and mms6 operons reveals a gene set
RT essential for magnetosome biogenesis in Magnetospirillum gryphiswaldense.";
RL J. Bacteriol. 196:2658-2669(2014).
CC -!- FUNCTION: Might phosphorylate lipids. {ECO:0000250|UniProtKB:P76407}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2W8P4}.
CC -!- INDUCTION: The last gene in the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- DISRUPTION PHENOTYPE: Normal magnetic response, normal magnetosomes
CC (PubMed:24816605). 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:24816605}.
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 diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDK99580.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; BX571797; CAE12046.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99580.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6NE47; -.
DR SMR; Q6NE47; -.
DR STRING; 1430440.MGMSRv2_2365; -.
DR EnsemblBacteria; CDK99580; CDK99580; MGMSRv2__2365.
DR KEGG; mgy:MGMSRv2__2365; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_1_3_5; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR Pfam; PF00781; DAGK_cat; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="Putative lipid kinase MamU"
FT /id="PRO_0000447771"
FT DOMAIN 43..131
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P76407"
FT BINDING 68..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76407"
SQ SEQUENCE 297 AA; 31995 MW; 8A4E6E2AE5C667EB CRC64;
MRIAAIINAR AGTVLRMSPS AVTERLSVVW GSLGHDAAII LAEGKDMGRM VRKACRDPDI
RAIIIGGGDG SLSRALEHVL ASGKSLGVLP LGTMNYMARQ IGMPLDLAQA AVALAGAVQT
PMDVGRVNDR YFLIRACFGA FPEFIQSRDR VRRKGGSFLE GALAGLSGVA RRYRIVEAEL
SSPGGRARIA TSFLMISNNL CRDSDPFLLE RERMDGGSLG VYVGRSAGPV GLMELGLQAA
MGRWASNEAL FQGEMHWLEV QTEQRKPLIS IDGEVEKMEG PFRFDILPGA LSILVPK
