MAMO_MAGSA
ID MAMO_MAGSA Reviewed; 637 AA.
AC Q2W8Q2;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable membrane transporter protein MamO {ECO:0000305};
GN Name=mamO; OrderedLocusNames=amb0969;
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 PROTEIN SEQUENCE OF 273-286, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE,
RP AND PROBABLE TOPOLOGY.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=27302060; DOI=10.1074/jbc.m116.731000;
RA Hershey D.M., Browne P.J., Iavarone A.T., Teyra J., Lee E.H., Sidhu S.S.,
RA Komeili A.;
RT "Magnetite biomineralization in Magnetospirillum magneticum is regulated by
RT a switch-like behavior in the HtrA protease MamE.";
RL J. Biol. Chem. 291:17941-17952(2016).
RN [3]
RP FUNCTION, 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 [4]
RP POSSIBLE FUNCTION AS A PROTEASE, AND MUTAGENESIS OF HIS-116; ASP-149 AND
RP THR-225.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=21414040; DOI=10.1111/j.1365-2958.2011.07631.x;
RA Quinlan A., Murat D., Vali H., Komeili A.;
RT "The HtrA/DegP family protease MamE is a bifunctional protein with roles in
RT magnetosome protein localization and magnetite biomineralization.";
RL Mol. Microbiol. 80:1075-1087(2011).
RN [5]
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 [6] {ECO:0007744|PDB:5HM9, ECO:0007744|PDB:5HMA}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 78-268, FUNCTION, COFACTOR,
RP DOMAIN, PROTEOLYTIC CLEAVAGE, DISRUPTION PHENOTYPE, PUTATIVE TOPOLOGY, AND
RP MUTAGENESIS OF HIS-116; HIS-148; ASP-149; THR-225 AND HIS-263.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=26981620; DOI=10.1371/journal.pbio.1002402;
RA Hershey D.M., Ren X., Melnyk R.A., Browne P.J., Ozyamak E., Jones S.R.,
RA Chang M.C., Hurley J.H., Komeili A.;
RT "MamO is a repurposed serine protease that promotes magnetite
RT biomineralization through direct transition metal binding in magnetotactic
RT bacteria.";
RL PLoS Biol. 14:E1002402-E1002402(2016).
CC -!- FUNCTION: Plays 2 roles; promotes magnetite nucleation/formation and
CC activates the MamE protease (Probable). Despite its near conservation
CC of a protease-like sequence, this is probably not a protease
CC (PubMed:26981620) (Probable). Required in conjunction with MamP for
CC proteolysis of at least MamE, itself and MamP (PubMed:26981620). May
CC transport a solute that controls MamE's protease activity. May place
CC individual iron atoms into the magnetite lattice (Probable).
CC {ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:20212111,
CC ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:26981620}.
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Evidence={ECO:0000305|PubMed:26981620};
CC Note=Binds to transition metal ions via His-148 and His-263, but also
CC binds metal via other residues. {ECO:0000269|PubMed:26981620};
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000269|PubMed:27302060}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:27302060}.
CC -!- INDUCTION: Part of the probable 18 gene mamAB operon.
CC {ECO:0000305|PubMed:20212111}.
CC -!- DOMAIN: The N-terminal region is an inactive protease, the C-terminal
CC region may have transporter activity which could activate the MamE
CC protease. {ECO:0000305|PubMed:26981620}.
CC -!- PTM: Subject to proteolytic cleavage by MamE.
CC {ECO:0000269|PubMed:26981620, ECO:0000269|PubMed:27302060}.
CC -!- DISRUPTION PHENOTYPE: Cells have no magnetic response but still make
CC empty magnetosome membranes; magnetosome proteins MamA and MamE
CC localize normally (PubMed:20212111). Deletion of genes mamH to mamV
CC (amb0961 to amb0978) gives cells with no magnetosomes and no magnetic
CC 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: There is a paralogous gene with partially overlapping
CC function in the genome (amb1004, called limO, AC Q2W8L7). LimO does not
CC encode the C-terminal TSUP domain and does not complement a mamO
CC deletion. {ECO:0000305|PubMed:21414040}.
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: 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}.
CC -!- CAUTION: Initally suggested to be a protease, mutation of the protease
CC domain active site residues does not alter its in vivo function in
CC magnetosome formation. {ECO:0000269|PubMed:26981620,
CC ECO:0000305|PubMed:21414040}.
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DR EMBL; AP007255; BAE49773.1; -; Genomic_DNA.
DR RefSeq; WP_011383400.1; NC_007626.1.
DR PDB; 5HM9; X-ray; 2.60 A; A=78-266.
DR PDB; 5HMA; X-ray; 2.30 A; A=78-268.
DR PDBsum; 5HM9; -.
DR PDBsum; 5HMA; -.
DR AlphaFoldDB; Q2W8Q2; -.
DR SMR; Q2W8Q2; -.
DR STRING; 342108.amb0969; -.
DR EnsemblBacteria; BAE49773; BAE49773; amb0969.
DR KEGG; mag:amb0969; -.
DR HOGENOM; CLU_409275_0_0_5; -.
DR OMA; YGMYLIR; -.
DR OrthoDB; 137454at2; -.
DR Proteomes; UP000007058; 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 3D-structure; Biomineralization; Direct protein sequencing; Magnetosome;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..637
FT /note="Probable membrane transporter protein MamO"
FT /id="PRO_0000447781"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..352
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26981620,
FT ECO:0000305|PubMed:27302060"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..416
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..517
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..554
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 576..586
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 78..268
FT /note="Protease-like"
FT /evidence="ECO:0000269|PubMed:26981620"
FT REGION 370..637
FT /note="TSUP-like"
FT /evidence="ECO:0000305|PubMed:26981620"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:26981620"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:26981620"
FT MUTAGEN 116
FT /note="H->A: Nearly complete loss of magnetic response when
FT amb1002 to amb1007 are also deleted, makes small magnetite
FT crystals at 30 degrees Celsius. At room temperature has
FT less effect. Complete loss of magnetic response; when
FT associated with A-149 and A-225."
FT /evidence="ECO:0000269|PubMed:21414040,
FT ECO:0000269|PubMed:26981620"
FT MUTAGEN 148
FT /note="H->A: Loss of magnetic response, no crystal
FT formation when amb1002 to amb1007 are also deleted.
FT Slightly improved Ni(2+) binding; when associated with A-
FT 263."
FT /evidence="ECO:0000269|PubMed:26981620"
FT MUTAGEN 149
FT /note="D->A: Nearly complete loss of magnetic response when
FT amb1002 to amb1007 are also deleted, makes small magnetite
FT crystals at 30 degrees Celsius. At room temperature almost
FT no effect. Complete loss of magnetic response when amb1002
FT to amb1007 are also deleted; when associated with A-116 and
FT A-225."
FT /evidence="ECO:0000269|PubMed:21414040,
FT ECO:0000269|PubMed:26981620"
FT MUTAGEN 225
FT /note="T->A: Wild-type magnetic response when amb1002 to
FT amb1007 are also deleted, makes normal magnetite crystals
FT at 30 degrees Celsius and room temperature. Complete loss
FT of magnetic response; when associated with A-116 and A-
FT 149."
FT /evidence="ECO:0000269|PubMed:21414040,
FT ECO:0000269|PubMed:26981620"
FT MUTAGEN 263
FT /note="H->A: Loss of magnetic response, no crystal
FT formation when amb1002 to amb1007 are also deleted.
FT Slightly improved Ni(2+) binding; when associated with A-
FT 148."
FT /evidence="ECO:0000269|PubMed:26981620"
SQ SEQUENCE 637 AA; 66343 MW; 7E216859494C9BF1 CRC64;
MIEVGETMGE LPTNKIVFCE RSWKTPVSIL AFLIFVTFAW GIYLLDHYDE DDNFHGADDL
SVGQFLVRNI AMPHVQRLYH TVPPAVVGVG GGGVNAGPVA SGAIVGTNGY VITTLHSVSK
LPEISVQVAT TGGIRRFPAQ VVKTIPGHDL ALLKMQTTEK FLHFRMADVQ TVVPGQQVFA
FGRNMAGAPL VRQGLVQSAD APLAVGATQI THLLRSDAVY SWEQTGGPLV NAQGDLVGIN
IAATGPTGKV EGFTVPAQVI VSHLQDVVRF KKGSATAPGQ PQTQTVAAGS TNWWSKARAV
VGGPTAIPGM GMNVVQGNVV KGNVAPSIPS GMPFIDTDHV GGAKIGGYSV ADIVGLVMLA
LAAGVTGGMM TMGGGVLQVA GMMVFFGYGM YLIRPVVFLT NVVVYGAASL RNDKAQLVQW
DKVKPLIPWG IAGVILGYFI GNAIGDSVVG ILLGLFALIM AGKAVMEILQ PNAGEETAES
ISATEAEDEM DELMALADGT SRPKASGLAL PEGHARSAVL GLPMGLFSGI LGISGGVIEV
PLQRYVGRIS LQNAIANSSV LVFWASVAGS VVAFLHGSST GLIHWEAPVT LALVMIPGAY
VGGIIGARLM RVLPVRVLKG VYAATMAAIA LKMLTSV
