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MAMH_MAGGM
ID   MAMH_MAGGM              Reviewed;         428 AA.
AC   Q6NE63; V6F5J8;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Magnetosome protein MamH {ECO:0000305};
DE   AltName: Full=Probable magnetosome permease MamH {ECO:0000305};
GN   Name=mamH {ECO:0000303|PubMed:13129949}; OrderedLocusNames=MGMSRv2__2381;
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 [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   [3]
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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX   PubMed=23889511; DOI=10.1111/mmi.12317;
RA   Raschdorf O., Mueller F.D., Posfai M., Plitzko J.M., Schueler D.;
RT   "The magnetosome proteins MamX, MamZ and MamH are involved in redox control
RT   of magnetite biomineralization in Magnetospirillum gryphiswaldense.";
RL   Mol. Microbiol. 89:872-886(2013).
CC   -!- FUNCTION: Required for correct biomineralization of the magnetosome;
CC       probably transports some form of iron. Partially functionally redundant
CC       with MamZ. {ECO:0000269|PubMed:23889511}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000250|UniProtKB:Q2W8R0}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: The first gene in the probable 17 gene mamAB operon.
CC       {ECO:0000305|PubMed:13129949}.
CC   -!- DISRUPTION PHENOTYPE: Slight decrease in magnetic response, has about
CC       30% fewer magnetosomes which are about 40% smaller than wild-type.
CC       Double mamH-mamZ deletion cells have a poor magnetic response and very
CC       few wild-type crystals; most cells have flake-like crystals
CC       (PubMed:23889511). 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:23889511}.
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 major facilitator superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CDK99596.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BX571797; CAE12030.1; -; Genomic_DNA.
DR   EMBL; HG794546; CDK99596.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6NE63; -.
DR   SMR; Q6NE63; -.
DR   STRING; 1430440.MGMSRv2_2381; -.
DR   TCDB; 2.A.1.43.1; the major facilitator superfamily (mfs).
DR   EnsemblBacteria; CDK99596; CDK99596; MGMSRv2__2381.
DR   KEGG; mgy:MGMSRv2__2381; -.
DR   eggNOG; COG2211; Bacteria.
DR   HOGENOM; CLU_642213_0_0_5; -.
DR   Proteomes; UP000018922; 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: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; IPR036259; MFS_trans_sf.
DR   InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR   Pfam; PF07690; MFS_1; 2.
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..428
FT                   /note="Magnetosome protein MamH"
FT                   /id="PRO_0000447744"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1
FT                   /note="M -> MTGM (in Ref. 2; CDK99596)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  45666 MW;  4D5B25C4741C5519 CRC64;
     MEPGRSEVEG HQRNALYLLS ALCMVFMTLV VAIQPLFLRN VLNIPFETAG AVNANVQVVT
     EVLDLFIFAY LGYLSDRIGR VRIIVAGFLV AAVGAVIAPL SPWVGGASIG ALVVYYVSRV
     IMSAGSGAVW PQLSALAGDF SDDSNRARLL SNTAFMMAFG VTLVYAVLMQ IPGHAGITVT
     MLLTAAISVA GAWLARKFLV DVAPRTVETS VPWRAVWDLV KAEPRLRLAF ASSLFARSDM
     VFVGLFLMLW FIYFADLVKV GQAEAAARAG MLIGLMGAVV MLSIPVWRSF IERFGRIQAV
     LLGMMLSALG FIMLGFVVNP FDGFIVFPIL LVSAGQAGCF VAPQILTVDH APKDLLGSVL
     GAFNVIGCLG IIFFVQIGGF LFDYIGPPAP FIFTGVGNLI ISAYALRLVK SEARGVGGGN
     TPGDDEVA
 
 
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