MAMN_MAGGM
ID MAMN_MAGGM Reviewed; 437 AA.
AC Q6NE56; V6F2B1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Magnetosome protein MamN {ECO:0000305};
DE AltName: Full=Putative ion transporter MamN {ECO:0000305};
GN Name=mamN {ECO:0000303|PubMed:13129949};
GN OrderedLocusNames=MGMSRv2__2374MGMSRv2__2374; ORFNames=mgI492, MGR_4096;
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 [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 [3]
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 [4]
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 [5]
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 [6]
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).
RN [7]
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 [8]
RP FUNCTION, 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 a role in biomineralization; might regulate pH in the
CC magnetosome. {ECO:0000305|PubMed:24816605,
CC ECO:0000305|PubMed:27286560}.
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 -!- DISRUPTION PHENOTYPE: Weak magnetic response, very few, small
CC magnetite-containing magnetosomes. Near wild-type localization of MamC
CC (PubMed:24816605). Magnetosome vesicles are approximately wild-type in
CC size, shape and chain-like alignment, only a few have crystals
CC (PubMed:27286560). 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, ECO:0000269|PubMed:27286560}.
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 arsenite-antimonite (ArsB) efflux (TC
CC 2.A.45) family. {ECO:0000305}.
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DR EMBL; BX571797; CAE12037.1; -; Genomic_DNA.
DR EMBL; AM085146; CAJ30121.1; -; Genomic_DNA.
DR EMBL; CU459003; CAM78028.1; -; Genomic_DNA.
DR EMBL; HG794546; CDK99589.1; -; Genomic_DNA.
DR RefSeq; WP_024080585.1; NZ_CP027526.1.
DR AlphaFoldDB; Q6NE56; -.
DR SMR; Q6NE56; -.
DR STRING; 1430440.MGMSRv2_2374; -.
DR TCDB; 2.A.45.2.3; the arsenite-antimonite (arsb) efflux family.
DR EnsemblBacteria; CDK99589; CDK99589; MGMSRv2__2374.
DR KEGG; mgry:MSR1_03410; -.
DR KEGG; mgy:MGMSRv2__2374; -.
DR eggNOG; COG1055; Bacteria.
DR HOGENOM; CLU_011920_4_0_5; -.
DR OrthoDB; 626718at2; -.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR004680; Cit_transptr-like_dom.
DR Pfam; PF03600; CitMHS; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Ion transport; Magnetosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..437
FT /note="Magnetosome protein MamN"
FT /id="PRO_0000447742"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 437 AA; 46180 MW; DAA2B80795117661 CRC64;
MVGFITLAVF IATFAVIYRW AEGSHLAVLA GAAVLVVIGT ISGTYTPRMA VQSIYFETLA
LIFGMAAISA LLARSGVYAY LAAGTAELSQ GQGRWILVMM ALVTYGISLA SNSLITVAVV
VPVTLTVCFR TGIDPVPVII AEIIAANLGG SSTMIGDFPN MILASAGKLH FNDFIGGMMP
ACLILLAVTF LFFEYRQGDW KKAEIPVDLA WVRGEQLRYS DIDHRLLRYG LIIFFITVIG
LVLAGPLKVR PGWIAFVAGL TALALGRFKD EEFFSACGGS DILFFGGLFV MVGALTSVGI
LDWAVAWLEG VTAGHDRVRA ILLMWMAAGV TIFVGGGTSA AVFAPVAATL RLDGDGQAAW
WALALGIMAG SCAALSGATA GALAMNQYSG FVKRHPELAS AAAAGLQFTH REYVRWGLPL
MGIFLVLSTV YIAVLAG
