ID F7XVE8_MIDMI Unreviewed; 617 AA.
AC F7XVE8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Phosphoglycerol transferase {ECO:0000313|EMBL:AEI88647.1};
DE EC=2.7.8.20 {ECO:0000313|EMBL:AEI88647.1};
GN Name=mdoB {ECO:0000313|EMBL:AEI88647.1};
GN OrderedLocusNames=midi_00337 {ECO:0000313|EMBL:AEI88647.1};
OS Midichloria mitochondrii (strain IricVA).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Midichloria.
OX NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88647.1, ECO:0000313|Proteomes:UP000006639};
RN [1] {ECO:0000313|EMBL:AEI88647.1, ECO:0000313|Proteomes:UP000006639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IricVA {ECO:0000313|EMBL:AEI88647.1,
RC ECO:0000313|Proteomes:UP000006639};
RX PubMed=21690562; DOI=10.1093/molbev/msr159;
RA Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT the free-living mitochondrial ancestor.";
RL Mol. Biol. Evol. 28:3285-3296(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP002130; AEI88647.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XVE8; -.
DR STRING; 696127.midi_00337; -.
DR KEGG; mmn:midi_00337; -.
DR HOGENOM; CLU_014653_1_0_5; -.
DR Proteomes; UP000006639; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008960; F:phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase activity; IEA:UniProtKB-EC.
DR CDD; cd16015; LTA_synthase; 1.
DR Gene3D; 3.30.1120.80; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012160; LtaS-like.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR47371; LIPOTEICHOIC ACID SYNTHASE; 1.
DR PANTHER; PTHR47371:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Manganese {ECO:0000256|PIRSR:PIRSR005091-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR005091-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006639};
KW Transferase {ECO:0000313|EMBL:AEI88647.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..531
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 310
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 310
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 479
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 480
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 617 AA; 71656 MW; 400EB992D9CDE673 CRC64;
MYKLTEFSET FRVEFFLFFF IQVALRLYLL SISDTDSISF LNYITIFSYG FLYDLVTFGW
ILLVLSLTTL IWLTQEEIII FKILRFFVFF TFILIIFLAT TSEIIFWYEF KSRFNFIAVD
YLVYTDEVIK NLMQSYAFIE ILIGLSIGSL MTAVVLFKFL KTTINGNRLL PFAILVLFNF
ASYSFVNNDL VNSDNRYINE ISKNGLYSLF SAYFHNDLSY EEFYVTLDEP ARFNILQSKF
KQNFHEGSII RSLKSTVKEK KHNIVIIIVE SLSAEFLSAF GNTLNITPYL DDLKDKSVFF
TNMYATGTRT VYGLAAITLS IPPIPGNSIV RRPENEDMFS LGGVLKAKGY HNQFVYGGFG
YFDNMNYFFQ NNGYQIIDRA DFKSKEVTFS NAWGVCDEDL LNKALREIDI LHEKSLPFFQ
VIMTTSNHRP FTFPAGRIDL TAQKRESAVK YTDYAIGKFL EEAKKKPWFD NTIFVIIADH
AASSCGKIAL DPNKHRIPLF LYAPKILTPK IINNLSSQID LAPTLLGILD IEYETQFYGL
DLLRENPNRA FISNYREMGY IENDKMVVLS PTRQKKFFIK DNEEQFVALE KEDKNLLETA
ISYFQTATNW RLYSKKH
//
