ID   MAMH_MAGSA              Reviewed;         431 AA.
AC   Q2W8R0;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Magnetosome protein MamH {ECO:0000305};
DE   AltName: Full=Probable magnetosome permease MamH {ECO:0000305};
GN   Name=mamH; OrderedLocusNames=amb0961;
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   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   [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).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=27481925; DOI=10.1128/jb.00280-16;
RA   Arakaki A., Kikuchi D., Tanaka M., Yamagishi A., Yoda T., Matsunaga T.;
RT   "Comparative subcellular localization analysis of magnetosome proteins
RT   reveals a unique localization behavior of Mms6 protein onto magnetite
RT   crystals.";
RL   J. Bacteriol. 198:2794-2802(2016).
CC   -!- FUNCTION: Required for correct biomineralization of the magnetosome;
CC       probably transports some form of iron. Partially functionally redundant
CC       with MamZ. {ECO:0000250|UniProtKB:Q6NE63}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000269|PubMed:27481925}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Tagged protein forms straight lines with a punctate
CC       pattern extending along most of the cell associated with its inner
CC       curvature, in the correct position to be associated with magnetosomes,
CC       but longer than the usual chain. {ECO:0000269|PubMed:27481925}.
CC   -!- INDUCTION: First gene of the probable 18 gene mamAB operon.
CC       {ECO:0000305|PubMed:20212111}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, magnetic response is
CC       slightly reduced and magnetosome membrane formation is wild-type
CC       (PubMed:20212111). 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   -!- 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   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP007255; BAE49765.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W8R0; -.
DR   SMR; Q2W8R0; -.
DR   STRING; 342108.amb0961; -.
DR   EnsemblBacteria; BAE49765; BAE49765; amb0961.
DR   KEGG; mag:amb0961; -.
DR   HOGENOM; CLU_642213_0_0_5; -.
DR   OMA; CPLWGVL; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR   Pfam; PF07690; MFS_1; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR01035; TCRTETA.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Biomineralization; Ion transport; Iron; Iron transport; Magnetosome;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..431
FT                   /note="Magnetosome protein MamH"
FT                   /id="PRO_0000447745"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  46024 MW;  4F175F69986F7F2A CRC64;
     MSRVEAAAAE VKVRQHNALY LLSALCMVFM TLVVAIQPLF LRNVLNISFE TAGAVNANVQ
     VVTEVLDLFI FAYLGYLSDR IGRVRIIVAG FLVAAIGAVI APLSPWIGGA SIGALVVYYV
     SRVIMSAGSG AVWPQLSALA GDFSDDDTRA RLMSNTAFMM AFGVTLVYAV LMQIPAHAGI
     AVTMLLTAAV SLAGAWLAGK FLVDVAPRTQ ETSVPWRAVW SLVKAEPRLR LAFASSLFAR
     SDMVFVGLFL MLWFIYFADL IKVGQAEAAA RAGILIGLMG AVVMLSIPVW RSFIEHFGRI
     QAVLLGMVLS ALGFIMLGFI INPFDWFIVL PILLIASGQA GCFVAPQILT VDYAPRDLLG
     SVLGAFNVIG CIGIIFFVQV GGFLFDYVGP PAPFVFTGVG NLIISAYALR LLKREARDGG
     GDDAPGDDGV A