MAMZ_MAGGM
ID MAMZ_MAGGM Reviewed; 648 AA.
AC V6F4W4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Magnetosome protein MamZ {ECO:0000303|PubMed:23889511};
DE AltName: Full=Probable magnetosome permease MamZ;
GN Name=mamZ {ECO:0000303|PubMed:23889511}; OrderedLocusNames=MGMSRv2__2323;
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 [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 [2]
RP INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=20023033; DOI=10.1128/jb.01292-09;
RA Ding Y., Li J., Liu J., Yang J., Jiang W., Tian J., Li Y., Pan Y., Li J.;
RT "Deletion of the ftsZ-like gene results in the production of
RT superparamagnetic magnetite magnetosomes in Magnetospirillum
RT gryphiswaldense.";
RL J. Bacteriol. 192:1097-1105(2010).
RN [3]
RP PROBABLE OPERON, AND DISRUPTION PHENOTYPE.
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, PROBABLE OPERON, DOMAIN, 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).
RN [5]
RP INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=24020498; DOI=10.1186/1471-2180-13-203;
RA Yang J., Li S., Huang X., Li J., Li L., Pan Y., Li Y.;
RT "MamX encoded by the mamXY operon is involved in control of magnetosome
RT maturation in Magnetospirillum gryphiswaldense MSR-1.";
RL BMC Microbiol. 13:203-203(2013).
RN [6]
RP POSSIBLE FUNCTION, PROBABLE INTERACTION WITH FTSZ-LIKE AND MAMY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1;
RX PubMed=30367002; DOI=10.1128/aem.02394-18;
RA Wang Q., Wu S., Li X., Zhang T., Yang J., Wang X., Li F., Li Y., Peng Y.,
RA Li J.;
RT "Work Patterns of MamXY Proteins during Magnetosome Formation in
RT Magnetospirillum gryphiswaldense MSR-1.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
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 (PubMed:23889511). May
CC function with MamX, MamY amd Mms6 in biomineralization (Probable).
CC Despite its strong similarity to MsrQ (AC V6EX82) this protein does not
CC genetically interact with bona fide MsrP (AC V6F0A4), which is encoded
CC elsewhere in the genome (PubMed:23889511).
CC {ECO:0000269|PubMed:23889511, ECO:0000305|PubMed:30367002}.
CC -!- SUBUNIT: Probably interacts with FtsZ-like and MamY proteins.
CC {ECO:0000269|PubMed:30367002}.
CC -!- SUBCELLULAR LOCATION: Magnetosome membrane
CC {ECO:0000250|UniProtKB:Q2W8K5, ECO:0000305|PubMed:23889511,
CC ECO:0000305|PubMed:30367002}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expressed in exponential phase, peaks about 18 hours. The
CC most highly expressed gene in this operon (PubMed:20023033,
CC PubMed:24020498). Protein is associated with magnetosomes at mid-
CC development then decreases (at protein level) (PubMed:30367002). Third
CC gene in the 4 gene mamXY operon (PubMed:20023033) (Probable).
CC {ECO:0000269|PubMed:20023033, ECO:0000269|PubMed:24020498,
CC ECO:0000269|PubMed:30367002, ECO:0000305|PubMed:22043287,
CC ECO:0000305|PubMed:23889511, ECO:0000305|PubMed:24020498}.
CC -!- DOMAIN: Deletion of the C-terminal 'ferric reductase' domain (residues
CC 444-645) phenocopies the deletion mutant; makes a magnetosome with
CC normal crystals sandwiched between flake-like crystals.
CC {ECO:0000269|PubMed:23889511}.
CC -!- DISRUPTION PHENOTYPE: Slightly reduced magnetic response, produces
CC chains of wild-type magnetite crystals sandwiched between irregularly
CC shaped, small flake-like crystals. The flake-like crystals are hematite
CC not magnetite. Phenotype is exacerbated when grown in NH(4)(+) instead
CC of NO(3)(-) medium. Double mamH-mamZ deletion cells have a poor
CC magnetic response and very few wild-type crystals; most cells have
CC flake-like crystals (PubMed:23889511). Deletion of 4 consecutive genes
CC (mamY, mamX, mamZ, ftsZm) leads to cells with an intermediate magnetic
CC response where magnetosomes have short chains of nearly regularly
CC shaped, cubo-octahedral crystals flanked by small particles with poorly
CC defined morphologies (PubMed:22043287). {ECO:0000269|PubMed:22043287,
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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the major facilitator
CC superfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305|PubMed:23889511}.
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DR EMBL; HG794546; CDK99538.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F4W4; -.
DR STRING; 1430440.MGMSRv2_2323; -.
DR EnsemblBacteria; CDK99538; CDK99538; MGMSRv2__2323.
DR KEGG; mgy:MGMSRv2__2323; -.
DR eggNOG; COG2717; Bacteria.
DR HOGENOM; CLU_426294_0_0_5; -.
DR Proteomes; UP000018922; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0110146; C:magnetosome membrane; ISS: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 1: Evidence at protein level;
KW Biomineralization; Ion transport; Iron; Iron transport; Magnetosome;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..648
FT /note="Magnetosome protein MamZ"
FT /id="PRO_0000447746"
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..431
FT /note="Major facilitator domain"
FT /evidence="ECO:0000305"
FT REGION 444..645
FT /note="Ferric reductase-like domain, required for correct
FT magnetite crystal formation"
FT /evidence="ECO:0000269|PubMed:23889511"
SQ SEQUENCE 648 AA; 70543 MW; 25183EAF642E7D42 CRC64;
MLEAWMPKSG KPSTGTTPAD FAPTQWNIIY LLMTVGSLVA ALSISIQPLL LDKIFGIAFE
KEGAVNADIQ VVAEIVSIVC VGWFGLLSDR IGRVRIIATG FLIAVAGAAM SLLSLQIGLA
FGAAGLVLFY LTRVLLTVGA DTVQLQLSTL VGDVSSRANR PRLMGNLVFM MVFGGTMLSA
IIMQMADYKG GVFIIMCLPL LIGIAGFQMT RESLRDVAQP QQAPTGDEHP LRQVWSVITS
DPRLQLAFAA AFYTRADVII LSLFFSLWCI SVSDLVGVTR TYATAHAAVM IGLLGLAVLA
AIPLWRSFIE RHSRISAIGA SLSLAAVGYI WLGMFANPFN WLVALPLLMV GIGHAGCFVT
LQVLTVDVSP KPILGAMVGA GYLVGGLGTV MLVQSGGYYF DALGPRAPFI LMGTGKMLVT
LYAAWLLANG IDETCDHHLK STRKVDWKPL VFLTAALPFV WLIGRSVIEG YFSNGSLGEA
PVGFVNRYLG DWAFTFLIIS LSMRPVQEIT GIKSLAKYRR MIGLFAFFYA VLHVLAYVTL
EWALNLGDMA SDIYKRPFIL LGLAAFLLLI PLAFTSTNSQ IKKIGGKRWK RLHRATYVIN
ALVALHFILA ANHENGEPYV YAAAVIVLLW YRFYQWRGGN VLRALRIG
