MAMZ_MAGSA
ID MAMZ_MAGSA Reviewed; 644 AA.
AC Q2W8K5;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Magnetosome protein MamZ {ECO:0000305};
DE AltName: Full=Probable magnetosome permease MamZ;
GN Name=mamZ {ECO:0000303|PubMed:27481925}; OrderedLocusNames=amb1016;
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 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 converts and then transports some form of iron. It is
CC partially functionally redundant with MamH. May function with MamX,
CC MamY amd Mms6. {ECO:0000250|UniProtKB:V6F4W4}.
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 -!- 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 -!- SIMILARITY: In the N-terminal section; belongs to the major facilitator
CC superfamily. {ECO:0000305}.
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DR EMBL; AP007255; BAE49820.1; -; Genomic_DNA.
DR RefSeq; WP_008615077.1; NC_007626.1.
DR AlphaFoldDB; Q2W8K5; -.
DR SMR; Q2W8K5; -.
DR STRING; 342108.amb1016; -.
DR TCDB; 2.A.1.43.2; the major facilitator superfamily (mfs).
DR EnsemblBacteria; BAE49820; BAE49820; amb1016.
DR KEGG; mag:amb1016; -.
DR HOGENOM; CLU_426294_0_0_5; -.
DR OMA; RYLGDWA; -.
DR OrthoDB; 626204at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0110146; C:magnetosome membrane; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
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 GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1250.20; -; 1.
DR HAMAP; MF_01207; MsrQ; 1.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR022837; MsrQ-like.
DR PANTHER; PTHR36964; PTHR36964; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF07690; MFS_1; 1.
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..644
FT /note="Magnetosome protein MamZ"
FT /id="PRO_0000447747"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..427
FT /note="Major facilitator domain"
FT /evidence="ECO:0000305"
FT REGION 488..599
FT /note="Ferric reductase-like domain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 69799 MW; C91F994D606795FA CRC64;
MPRNAEAPAK GTTADDFAPT QWNIIYLLMT VGALMAALSI SIQPLLLDKI FGIAFEKEGA
VNADIQVVAE IVSIVCVGWF GLLSDRIGRV RIIALGFLIA VVGAAVSLLS LQVGLAFGAA
GLVLFYLTRV LLTVGADTVQ LQLSTLVGDV SSRANRPRLM GNLVFMMVFG GTMLAAIVMQ
MADYPGGVFL IMCLPLLAGI AGFQLTRRNL RDVAPPQPAS EDDEHPLRQV WTVITSDPRM
QLAFAAAFYT RADVIILSLF FSLWCISVSD LVGVTRTFAT AHAAVMIGLL GLAVLAAVPL
WRSFIERHSR ISAIGASLSL AALGYIWLGM FANPFNWLVA LPLLMVGIGH AGCFVTLQVL
TVDASPKPIL GAMVGAGYLV GGLGTVMLVQ SGGYYFDALG PRAPFILMGT GKMLVTLYAA
WLLANGIDET CDHHLKSART VDWKPLVFLT AALPFVWLVG RSVIEGYISN GSLGEAPVGF
VNRYLGDWAF TFLIISLAMR PVQEITGIKT LAKYRRMIGL FAFFYAVMHV LAYVALEWAL
NLGDMMGDIY KRPFILLGLV AFALLIPLAF TSANSQIKRI GGKRWKKLHS ATYVINALVA
LHFILAANHE NGEPYVYAAA VIVLLWYRFH QWRGGNVLRA LRIG
