ID   MAMY_MAGSA              Reviewed;         389 AA.
AC   Q2W8K3;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Liposome tubulation protein MamY {ECO:0000303|PubMed:20345667};
GN   Name=mamY {ECO:0000303|PubMed:20345667}; OrderedLocusNames=amb1018;
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   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND LIPOSOME-BINDING.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=20345667; DOI=10.1111/j.1365-2958.2010.07117.x;
RA   Tanaka M., Arakaki A., Matsunaga T.;
RT   "Identification and functional characterization of liposome tubulation
RT   protein from magnetotactic bacteria.";
RL   Mol. Microbiol. 76:480-488(2010).
RN   [3]
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).
RN   [4]
RP   FUNCTION, AND BINDS CARDIOLIPIN.
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=30039923; DOI=10.1002/biot.201800087;
RA   Tanaka M., Suwatthanarak T., Arakaki A., Johnson B.R.G., Evans S.D.,
RA   Okochi M., Staniland S.S., Matsunaga T.;
RT   "Enhanced Tubulation of Liposome Containing Cardiolipin by MamY Protein
RT   from Magnetotactic Bacteria.";
RL   Biotechnol. J. 13:E1800087-E1800087(2018).
CC   -!- FUNCTION: Causes tubulation when added to magnetosome-derived
CC       liposomes, binds liposomes; may be involved in constriction of the cell
CC       inner membrane to form mature magnetosomes (PubMed:20345667). Binds
CC       preferentially to cardiolipin, a component of bacterial membranes, with
CC       very poor to no binding of other tested (phospho)lipids. Addition of
CC       cardiolipin to magnetosome-derived lipids increases tubulation
CC       (PubMed:30039923). May function with MamX, MamZ amd Mms6 (By
CC       similarity). {ECO:0000250|UniProtKB:V6F5F3,
CC       ECO:0000269|PubMed:20345667, ECO:0000269|PubMed:30039923}.
CC   -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC       {ECO:0000269|PubMed:20345667}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Primarily associated with immature magnetosomes
CC       with small magnetite crystals, but longer than the usual magnetosome
CC       chain. {ECO:0000269|PubMed:20345667, ECO:0000269|PubMed:27481925}.
CC   -!- DISRUPTION PHENOTYPE: No growth phenotype, retains a magnetic response.
CC       Magnetosome vesicles are slightly bigger than wild-type while magnetite
CC       crystals are equal in number but have a much wider size range.
CC       {ECO:0000269|PubMed:20345667}.
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: Belongs to the magnetosome MamY family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007255; BAE49822.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W8K3; -.
DR   EnsemblBacteria; BAE49822; BAE49822; amb1018.
DR   KEGG; mag:amb1018; -.
DR   HOGENOM; CLU_882247_0_0_5; -.
DR   OMA; RCAEDTE; -.
DR   OrthoDB; 453796at2; -.
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:0008289; F:lipid binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Biomineralization; Lipid-binding; Magnetosome; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..389
FT                   /note="Liposome tubulation protein MamY"
FT                   /id="PRO_0000447813"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..62
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  42567 MW;  A306A4F94C32AFD1 CRC64;
     MAIAAIMGDV LMLMGFNKAA FGKLNSASRA ALIGAVIWAV LSIVYLTIFN GWKNLFTMLP
     HEFFIVLLSI ALPIGLTVLI LMLSRIVKSV DTLKSEVTTL SRNDVSSEGS VAMLADLFRE
     HRAAIAAQVE AQVEATTQLI RLNQEGRALA APAQASGTDE AMTLLAQLFR EHREAVAAQL
     EAQASATAQL VQVTRDSRDG IVDELRSQRV LSQEITQELS QITQSRTVAP APPGLDPSQR
     IDRMRALAEV LGLALNDLSM TATQVLTEHL NAAHGDRDGT RKFISTLTTA YFAGDKNVFF
     RSLVQEAVNR SEQLRRCAED TESVRQQISK ILREAREIRS LVAACDPNDL VRIVFEDGEL
     WALEKALAEH FLIDGSPVWT ETAPDSGMD