ID   MAMV_MAGSA              Reviewed;         333 AA.
AC   Q2W8P3;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Putative transporter MamV {ECO:0000305};
GN   Name=mamV {ECO:0000303|PubMed:20212111}; OrderedLocusNames=amb0978;
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   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).
CC   -!- FUNCTION: Expression of just the minimal mamAB gene cluster (amb0961 to
CC       amb0978), including this gene, is sufficient to form a minimal
CC       magnetosome chain with small magnetite particles.
CC       {ECO:0000269|PubMed:22716969}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Last member 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   -!- MISCELLANEOUS: This protein has no ortholog in M.gryphiswaldense strain
CC       MSR-1. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. {ECO:0000305}.
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DR   EMBL; AP007255; BAE49782.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W8P3; -.
DR   SMR; Q2W8P3; -.
DR   EnsemblBacteria; BAE49782; BAE49782; amb0978.
DR   KEGG; mag:amb0978; -.
DR   HOGENOM; CLU_013430_3_3_5; -.
DR   OMA; NYGHEKA; -.
DR   OrthoDB; 381612at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1510.10; -; 1.
DR   Gene3D; 3.30.70.1350; -; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027470; Cation_efflux_CTD.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   Pfam; PF16916; ZT_dimer; 1.
DR   SUPFAM; SSF160240; SSF160240; 1.
DR   SUPFAM; SSF161111; SSF161111; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..333
FT                   /note="Putative transporter MamV"
FT                   /id="PRO_0000447741"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   333 AA;  35606 MW;  69BCE73D9BD8F2F3 CRC64;
     MLGRPMKPSK CQECRDRAAW LDMFTALALA VFKTALGVLS GSMALQAHSL HSFGDFLTKG
     INLASVKLSS RPANSAFPYG YGKVQFLSAN FIGISLMAGA AAMLWYNVTH LGSGHVQVPE
     VWAVFGALIS AGTAELMHRY LRCVAEHTNS PAIMAAAADN RGDAYSSLAV LAGIVLSILG
     WVAADHLAAI LVSLLVLRIG AVIAWDSIHG LMDGSVPSHR IDGIRQLLAA HHPGVSVVDL
     RGRRMGETWE VDLQLSISSQ VTVEECHALT RELESRIARE EPHACHIRIR FIPQSGDATK
     TAVIETAAAV DEFAYLVEAS AALRPLGHSR NGG