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MAME_MAGSA
ID   MAME_MAGSA              Reviewed;         728 AA.
AC   Q2W8Q8;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Magnetosome formation protease MamE {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000305|PubMed:21414040};
DE   AltName: Full=Magnetochrome MamE {ECO:0000305};
DE   AltName: Full=Magnetosome serine protease MamE {ECO:0000305};
GN   Name=mamE; OrderedLocusNames=amb0963;
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   INDUCTION.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=20161777; DOI=10.1371/journal.pone.0009151;
RA   Rioux J.B., Philippe N., Pereira S., Pignol D., Wu L.F., Ginet N.;
RT   "A second actin-like MamK protein in Magnetospirillum magneticum AMB-1
RT   encoded outside the genomic magnetosome island.";
RL   PLoS ONE 5:E9151-E9151(2010).
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   PROBABLE FUNCTION AS A PROTEASE, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF HIS-188; ASP-221; SER-297 AND
RP   392-CYS--CYS-441.
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   POSSIBLE COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=23176475; DOI=10.1042/bst20120104;
RA   Siponen M.I., Adryanczyk G., Ginet N., Arnoux P., Pignol D.;
RT   "Magnetochrome: a c-type cytochrome domain specific to magnetotatic
RT   bacteria.";
RL   Biochem. Soc. Trans. 40:1319-1323(2012).
RN   [6]
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   [7]
RP   FUNCTION AS A PROTEASE, ACTIVITY REGULATION, PROBABLE TOPOLOGY, AND
RP   MUTAGENESIS OF GLN-294 AND SER-297.
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   [8]
RP   FUNCTION AS A PROTEASE, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF HIS-188;
RP   ASP-221 AND SER-297.
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: Acts at 2 distinct steps of magnetosome formation; required
CC       for correct localization of proteins to the magnetosome while the
CC       protease activity is required for maturation of small magnetite
CC       crystals into larger, functional ones. The 2 functions are separable by
CC       mutation (PubMed:21414040). Probably cleaves at least itself, MamO and
CC       MamP; cleavage requires the putative transport domain of MamO
CC       (Probable) (PubMed:26981620). Involved in localization of some proteins
CC       (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome
CC       (PubMed:20212111, PubMed:21414040). {ECO:0000269|PubMed:20212111,
CC       ECO:0000269|PubMed:21414040, ECO:0000269|PubMed:26981620,
CC       ECO:0000305|PubMed:21414040}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475};
CC       Note=Probably binds 2 heme groups via the 2 magnetochrome (MCR) motifs.
CC       {ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475};
CC   -!- ACTIVITY REGULATION: Autoproteolysis is stimulated by exogenous
CC       substrates or peptides that bind to its PDZ domains; may be stimulated
CC       by an environmental cue in vivo. Protease activity is tightly
CC       regulated; increasing its activity decreases substrate levels and
CC       disturbs biomineralization. {ECO:0000269|PubMed:27302060}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -32 mV. {ECO:0000269|PubMed:23176475};
CC   -!- SUBUNIT: Might interact with MamB via PDZ1.
CC       {ECO:0000250|UniProtKB:V6F2B6}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000269|PubMed:20161777, ECO:0000305|PubMed:21414040}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expressed during exponential phase in static growth
CC       conditions (PubMed:20161777). Part of the probable 18 gene mamAB operon
CC       (Probable). {ECO:0000269|PubMed:20161777, ECO:0000305|PubMed:20212111}.
CC   -!- PTM: Subject to autocatalytic cleavage; cleavage also requires MamO.
CC       {ECO:0000269|PubMed:26981620}.
CC   -!- DISRUPTION PHENOTYPE: Cells have no magnetic response but still make
CC       empty magnetosome membranes. Alterations in localization of magnetosome
CC       proteins; MamA is mislocalized to random foci near the cell membrane,
CC       while MamJ is more diffuse than in wild-type (PubMed:20212111).
CC       Alterations in localization of magnetosome proteins MamC, MamF and MamI
CC       (PubMed:21414040). Deletion of genes mamH to mamV (amb0961 to amb0978)
CC       gives cells with no magnetosomes and no magnetic response
CC       (PubMed:20212111). {ECO:0000269|PubMed:20212111,
CC       ECO:0000269|PubMed:21414040}.
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 are 2 paralogous genes in the genome; limE
CC       (amb1002) has a partially overlapping function with MamE, while mamE-
CC       like (amb0410) does not seem to play a role in biomineralization.
CC       {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   -!- MISCELLANEOUS: There is a third MCR motif in the M.gryphiswaldense
CC       strain MSR-1 MamE ortholog. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the peptidase S1C
CC       family. {ECO:0000305}.
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DR   EMBL; AP007255; BAE49767.1; -; Genomic_DNA.
DR   RefSeq; WP_011383396.1; NC_007626.1.
DR   AlphaFoldDB; Q2W8Q8; -.
DR   SMR; Q2W8Q8; -.
DR   STRING; 342108.amb0963; -.
DR   EnsemblBacteria; BAE49767; BAE49767; amb0963.
DR   KEGG; mag:amb0963; -.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OMA; CENCHQI; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0110146; C:magnetosome membrane; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR040963; MCR.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF18509; MCR; 2.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Biomineralization; Heme; Hydrolase; Iron;
KW   Magnetosome; Membrane; Metal-binding; Protease; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..728
FT                   /note="Magnetosome formation protease MamE"
FT                   /id="PRO_0000447779"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..728
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:27302060"
FT   DOMAIN          471..573
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          622..721
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   MOTIF           375..398
FT                   /note="MCR (magnetochrome) 1"
FT                   /evidence="ECO:0000305|PubMed:23176475"
FT   MOTIF           421..444
FT                   /note="MCR 2"
FT                   /evidence="ECO:0000305|PubMed:23176475"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0V0,
FT                   ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040"
FT   ACT_SITE        221
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0V0,
FT                   ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040"
FT   ACT_SITE        297
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0V0,
FT                   ECO:0000269|PubMed:26981620, ECO:0000305|PubMed:21414040"
FT   BINDING         392
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"
FT   BINDING         395
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"
FT   BINDING         396
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000305|PubMed:21414040, ECO:0000305|PubMed:23176475"
FT   BINDING         438
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000305|PubMed:21414040,
FT                   ECO:0000305|PubMed:23176475"
FT   BINDING         441
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000305|PubMed:21414040,
FT                   ECO:0000305|PubMed:23176475"
FT   BINDING         442
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000305|PubMed:21414040,
FT                   ECO:0000305|PubMed:23176475"
FT   MUTAGEN         188
FT                   /note="H->A: Some loss of magnetic response; when
FT                   associated with A-221 and A-297. Significant loss of
FT                   magnetic response, MamE, MamO, MamP no longer processed
FT                   when amb1002 to amb1007 are also deleted; when associated
FT                   with A-221 and A-297."
FT                   /evidence="ECO:0000269|PubMed:21414040,
FT                   ECO:0000269|PubMed:26981620"
FT   MUTAGEN         221
FT                   /note="D->A: Some loss of magnetic response; when
FT                   associated with A-188 and A-297. Significant loss of
FT                   magnetic response, MamE, MamO, MamP no longer processed
FT                   when amb1002 to amb1007 are also deleted; when associated
FT                   with A188 and A-297."
FT                   /evidence="ECO:0000269|PubMed:21414040"
FT   MUTAGEN         294
FT                   /note="Q->P: Increased protease activity, decreased
FT                   dependency on MamO, magnetic response lower than wild-type
FT                   but higher than deletion mutant."
FT                   /evidence="ECO:0000269|PubMed:27302060"
FT   MUTAGEN         297
FT                   /note="S->A: Loss of protease activity. Some loss of
FT                   magnetic response; when associated with A-188 and A-221.
FT                   Significant loss of magnetic response, MamE, MamO, MamP no
FT                   longer processed when amb1002 to amb1007 are also deleted;
FT                   when associated with A188 and A-221."
FT                   /evidence="ECO:0000269|PubMed:21414040,
FT                   ECO:0000269|PubMed:27302060"
FT   MUTAGEN         392..441
FT                   /note="CTTCHDLIPAGNGRPAPMMPIAAPIPPPPIPMGAVSPHTDGRQNMNCANC->
FT                   ATTAHDLIPAGNGRPAPMMPIAAPIPPPPIPMGAVSPHTDGRQNMNAANA: Removes
FT                   both putative heme-binding sites, partial loss of magnetic
FT                   response, significant loss of magnetic response when
FT                   amb1002 to amb1007 are also deleted. The latter mutant is
FT                   capable of making nearly wild-type size crystals, but makes
FT                   them less frequently and later than wild-type."
FT                   /evidence="ECO:0000269|PubMed:21414040"
SQ   SEQUENCE   728 AA;  73478 MW;  AA396F0AE33C69E0 CRC64;
     MAMFNGDVED GGRGDASCGK DLKRYLMLMG VVALVVLFGA FIYRQSSGGL RLGAMLEQMG
     RGTGPAVNVP VQQGGPSAAV NPAMSVPAGA RVAPPSAAGA IATMPPMVDF GPAPIGAGGP
     FSSVVTLLRN SVVAVTASSA NGQAMPDPLG LANPDGLPHF ANPATRSVEN IGTGVIVRND
     GFIVTNYHVV RGANSVFVTV QDDVGSTRYS AEIIKMDEAL DLALLKVAPK TPLTAAVLGD
     SDGVQVADEV IAIGTPFGLD MTVSRGIISA KRKSMVIEGV THSNLLQTDA AINQGNSGGP
     LVISNGTVVG INTAIYTPNG AFAGIGFAVP SNQARLFILD EVGWLPTSTA EGASMGLVAM
     QRPMGGGVGA AGPAIFAGTR APHTDGRQNM DCTTCHDLIP AGNGRPAPMM PIAAPIPPPP
     IPMGAVSPHT DGRQNMNCAN CHQMLGGAAP IAAPGLGGGA YRFAQPPGSL AINIQGPRGG
     QSTAAGTGRV TLLGAALTPM SQRLGAQTGV PVGRGVFISG VTPNTPAATA GLRPGDVLLK
     VDGRPVRLPE EVSAIMVEMH AGRSVRLGVL RDGDVRNMTL VAGPAGLAAA AVQAPAIADM
     AQPPMGGMAP TAPGMVAVPG GPAVMPKPPT EFNWLGMEIE TFQAPRPITG VPGAVPVPGA
     KGAQVAEVLV GSRAAVAGLQ ANDLILEVNN RPVAGPARLD AAIKGATNAG QQILLKVNRN
     GQEFWIVL
 
 
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