ID   MAMU_MAGSA              Reviewed;         297 AA.
AC   Q2W8P4;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Putative lipid kinase MamU {ECO:0000305};
DE            EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00783};
GN   Name=mamU; OrderedLocusNames=amb0977;
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   PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=20212111; DOI=10.1073/pnas.0914439107;
RA   Murat D., Quinlan A., Vali H., Komeili A.;
RT   "Comprehensive genetic dissection of the magnetosome gene island reveals
RT   the step-wise assembly of a prokaryotic organelle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:5593-5598(2010).
RN   [3]
RP   MINIMAL MAGNETOSOME ISLAND.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=22716969; DOI=10.1111/j.1365-2958.2012.08132.x;
RA   Murat D., Falahati V., Bertinetti L., Csencsits R., Koernig A., Downing K.,
RA   Faivre D., Komeili A.;
RT   "The magnetosome membrane protein, MmsF, is a major regulator of magnetite
RT   biomineralization in Magnetospirillum magneticum AMB-1.";
RL   Mol. Microbiol. 85:684-699(2012).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=27481925; DOI=10.1128/jb.00280-16;
RA   Arakaki A., Kikuchi D., Tanaka M., Yamagishi A., Yoda T., Matsunaga T.;
RT   "Comparative subcellular localization analysis of magnetosome proteins
RT   reveals a unique localization behavior of Mms6 protein onto magnetite
RT   crystals.";
RL   J. Bacteriol. 198:2794-2802(2016).
CC   -!- FUNCTION: Might phosphorylate lipids. {ECO:0000250|UniProtKB:P76407}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27481925}.
CC       Note=Tagged protein forms a diffuse intracellular stain.
CC       {ECO:0000269|PubMed:27481925}.
CC   -!- INDUCTION: Part of the probable 18 gene mamAB operon.
CC       {ECO:0000305|PubMed:20212111}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, magnetic response and
CC       magnetosome formation is wild-type (PubMed:20212111). Deletion of genes
CC       mamH to mamV (amb0961 to amb0978) gives cells with no magnetosomes and
CC       no magnetic response (PubMed:20212111). {ECO:0000269|PubMed:20212111}.
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: Expression of just the minimal mamAB gene cluster
CC       (amb0961 to amb0978), including this gene, is sufficient to form a
CC       minimal magnetosome chain with small magnetite particles.
CC       {ECO:0000269|PubMed:22716969}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AP007255; BAE49781.1; -; Genomic_DNA.
DR   RefSeq; WP_008622201.1; NC_007626.1.
DR   AlphaFoldDB; Q2W8P4; -.
DR   SMR; Q2W8P4; -.
DR   STRING; 342108.amb0977; -.
DR   EnsemblBacteria; BAE49781; BAE49781; amb0977.
DR   KEGG; mag:amb0977; -.
DR   HOGENOM; CLU_045532_5_0_5; -.
DR   OMA; RWASNEA; -.
DR   OrthoDB; 869726at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA: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_0000447772"
FT   DOMAIN          1..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;  31952 MW;  02C0A4563E1DA290 CRC64;
     MRIAAIINER AGTVACLSPP VVAARLSAIW TSLGHQAHVT LAEGKDMGRA IRKACRDPAV
     HAVIIGGGDG SLSRSLKHVV GSGKSLGVLP LGTMNYVARQ FGVPFDLDRA AVALADAVPT
     PTDLGRVNDR FFLIRACLGA FPEFIRSRDE ARRKGGSFLD GALAGLTGLA RGHRLIEAEL
     IGPDVQARIA TSFFMVSNNM CRDSDPFQLE RERMDGATLG VYIGQGAGPF SLMDLGLQVA
     MGRWASNEAL IRGSLPWLEI RTRQRKPLVS IDGEVEKMEA PFRFDILPGV LPMLVPK