MAMO_MAGGM
ID MAMO_MAGGM Reviewed; 632 AA.
AC Q93DZ1; V6F515;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable membrane transporter protein MamO {ECO:0000305};
GN Name=mamO {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2373;
GN ORFNames=mgI493, MGR_4097;
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].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=11571158; DOI=10.1128/aem.67.10.4573-4582.2001;
RA Grunberg K., Wawer C., Tebo B.M., Schuler D.;
RT "A large gene cluster encoding several magnetosome proteins is conserved in
RT different species of magnetotactic bacteria.";
RL Appl. Environ. Microbiol. 67:4573-4582(2001).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=14766587; DOI=10.1128/aem.70.2.1040-1050.2004;
RA Gruenberg K., Mueller E.C., Otto A., Reszka R., Linder D., Kube M.,
RA Reinhardt R., Schueler D.;
RT "Biochemical and proteomic analysis of the magnetosome membrane in
RT Magnetospirillum gryphiswaldense.";
RL Appl. Environ. Microbiol. 70:1040-1050(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=20674739; DOI=10.1016/j.resmic.2010.07.002;
RA Yang W., Li R., Peng T., Zhang Y., Jiang W., Li Y., Li J.;
RT "mamO and mamE genes are essential for magnetosome crystal
RT biomineralization in Magnetospirillum gryphiswaldense MSR-1.";
RL Res. Microbiol. 161:701-705(2010).
RN [8]
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 [9]
RP FUNCTION, MINIMAL VESICLE FORMATION GENES, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=27286560; DOI=10.1371/journal.pgen.1006101;
RA Raschdorf O., Forstner Y., Kolinko I., Uebe R., Plitzko J.M., Schueler D.;
RT "Genetic and Ultrastructural Analysis Reveals the Key Players and Initial
RT Steps of Bacterial Magnetosome Membrane Biogenesis.";
RL PLoS Genet. 12:E1006101-E1006101(2016).
CC -!- FUNCTION: Plays 2 roles; promotes magnetite nucleation/formation and
CC activates the MamE protease (By similarity) (PubMed:20674739). Despite
CC its near conservation of a protease-like sequence, this is probably not
CC a protease (By similarity). Required in conjunction with MamP for
CC proteolysis of at least MamE, itself and MamP (By similarity). May
CC transport a solute that controls MamE's protease activity. May place
CC individual iron atoms into the magnetite lattice (By similarity). One
CC of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis;
CC coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon
CC restores magnetosome vesicle formation but not magnetite biosynthesis
CC (PubMed:27286560). {ECO:0000250|UniProtKB:Q2W8Q2,
CC ECO:0000269|PubMed:20674739, ECO:0000269|PubMed:27286560}.
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Evidence={ECO:0000250|UniProtKB:Q2W8Q2};
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:14766587}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Part of the probable 17 gene mamAB operon.
CC {ECO:0000305|PubMed:13129949}.
CC -!- DOMAIN: The N-terminal region is an inactive protease, the C-terminal
CC region may have transporter activity which could contribute to its
CC function in proteolysis by MamE. {ECO:0000250|UniProtKB:Q2W8Q2}.
CC -!- PTM: Subject to proteolytic cleavage by MamE.
CC {ECO:0000250|UniProtKB:Q2W8Q2}.
CC -!- DISRUPTION PHENOTYPE: Single gene deletion, loss of magnetic response,
CC about 30% iron content. Forms magnetosome chains without magnetosome
CC crystals (PubMed:20674739). Deletion of approximately 80 kb of DNA,
CC including this operon, leads to cells that are non-magnetic, lack
CC internal membrane systems, grow poorly, have reduced mobility and take-
CC up and accumulate iron poorly (PubMed:13129949).
CC {ECO:0000269|PubMed:13129949, ECO:0000269|PubMed:20674739}.
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:11571158}.
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: In the N-terminal section; belongs to the peptidase S1C
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the 4-toluene
CC sulfonate uptake permease (TSUP) (TC 2.A.102) family. {ECO:0000305}.
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DR EMBL; AF374354; AAL09994.1; -; Genomic_DNA.
DR EMBL; BX571797; CAE12038.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30122.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78029.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99588.1; -; Genomic_DNA.
DR RefSeq; WP_024080584.1; NZ_CP027526.1.
DR AlphaFoldDB; Q93DZ1; -.
DR SMR; Q93DZ1; -.
DR STRING; 1430440.MGMSRv2_2373; -.
DR EnsemblBacteria; CDK99588; CDK99588; MGMSRv2__2373.
DR KEGG; mgry:MSR1_03420; -.
DR KEGG; mgy:MGMSRv2__2373; -.
DR eggNOG; COG0265; Bacteria.
DR eggNOG; COG0730; Bacteria.
DR HOGENOM; CLU_409275_0_0_5; -.
DR OrthoDB; 137454at2; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0110146; C:magnetosome membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR InterPro; IPR002781; TM_pro_TauE-like.
DR Pfam; PF01925; TauE; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Magnetosome; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..632
FT /note="Probable membrane transporter protein MamO"
FT /id="PRO_0000447780"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 78..268
FT /note="Protease-like"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q2"
FT REGION 365..632
FT /note="TSUP-like"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q2"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q2"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q2W8Q2"
SQ SEQUENCE 632 AA; 65380 MW; 915FFCAEBD856162 CRC64;
MIEIGETMGD QPTNKIVFCE RSWKAPVSIL AFLILVTFAW GAYLLDNYDE DDYFRGSDDM
SVGQFLVRNV AMPDVQRLYY TVPPAVVGVG GGGVNAGPVA SGAIVGANGY VITTLHSVAN
VPDITVQVAT SAGIRRFPAQ VVKTIPGHNL ALLKLQTTEK FLHFRMANIQ TVVPGQQVFA
FGRNMAGAPL VRQGMVQSSD APLAVGTTQI THLLRSDAVY SWEQTGGPLV NAQGDLVGIN
IAATGPTGKV EGFTVPAQVI VSHLQDVVRF KTGGAAGVAP PAAQTVAMGS SSWWSKAKAV
VGGPTAVPGM GMNVVQGTVT TGIPSGMPFV DTDHVGGAKI GGYSIADILG LGMLALAAGV
TGGMMTMGGG VLQVAGMMVF FGYGMYLIRP VVFLTNVVVY GAAALRNDKA QLVQWDKVKP
LIPWGVAGVV IGYFIGNAIG DSVVGVLLGL FALIMAGKAV LEILQPNAGE DTAEAIAAAE
AGDEMDELMA LAEGTTRPKT SGIALPEGPT RSAVLGLPMG LFSGILGISG GVIEVPLQRY
IGRISLQNAI ANSSVLVFWA SVAGSVVAFI HGGSTGLIHW EAPVTLALVM IPGAYVGGIL
GARLMRVLPV RVLKGIYAAT MAAIAIKMLT TV
