ID A0A0R2D3V7_9LACO Unreviewed; 731 AA.
AC A0A0R2D3V7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase {ECO:0000313|EMBL:KRM94483.1};
GN ORFNames=FC56_GL001440 {ECO:0000313|EMBL:KRM94483.1};
OS Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM94483.1, ECO:0000313|Proteomes:UP000051256};
RN [1] {ECO:0000313|EMBL:KRM94483.1, ECO:0000313|Proteomes:UP000051256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM94483.1,
RC ECO:0000313|Proteomes:UP000051256};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004936}.
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}.
CC -!- SIMILARITY: Belongs to the LTA synthase family.
CC {ECO:0000256|ARBA:ARBA00009983}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM94483.1}.
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DR EMBL; AYZR01000004; KRM94483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2D3V7; -.
DR STRING; 1423802.FC56_GL001440; -.
DR PATRIC; fig|1423802.4.peg.1458; -.
DR Proteomes; UP000051256; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16015; LTA_synthase; 1.
DR Gene3D; 3.30.1120.170; -; 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 3: Inferred from homology;
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:UP000051256};
KW Transferase {ECO:0000313|EMBL:KRM94483.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 270..566
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 703..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 498
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 499
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 731 AA; 82889 MW; 4E9754FF8A7901E7 CRC64;
MSASDKMEAA KFLRSISVKY LNNILKRSST RIGFIGLLTA CFWLKTMLAY IVDFRLGISN
PFQFLIVLIN PLATTVLLLG IALYFKKARY FYPIAIIIDI ANTVLLYLNV IYFREFTDFM
TVSTMTGYSK VNQGLSGSSL ALTNIHDVLY WLDLVIIISL LLARKIKIDK HPLNKRVGLA
VTSASILFFV FNLTLGEMDR PQLLTRTFDR TYIVKYLGID AFTVYDGLKS QHNNDLRATA
TKSELAKVKQ FTDNHYAKPN SKYYGIAKGK NVIVLHLESF QQFLIGQKIN GQEVTPFLNK
LYKSQSSYSF KNFFHQVGQG KTSDAENMME TSTYGLPQGS LFAQLGSDNT FQAAPAILNQ
RAGYSSAVFH GNIASFWNRN NVYKNLGYQY FFDASYYDTT GDRSLGYGLK DKLLFRDSVP
YFENLQQPFY AKYITVTNHF PYDLDKEDTN FKTTNTGDSA VDNYFLTAHY LDQSIREFYS
YLKKTGMLKN SVIVLYGDHY GISNSENKSL AKALGKDPDK WNDFDNASMQ RVPYIINIPG
QTNGRIFDEY AGEIDALPTL MHLLGISSKR YIQFGTDVFS KQHDQLVAFR NKDWVSPKYT
SIDGTVYDSA SGKEIVNPSK AQTKLFKAND AKVDNELNLS DSLNEKNLLR FYHPKGFKNI
NPSDFNYANG LSKERKIEKE LGNKSTSLFS ENGNKSTLSD YVTNAPEVSH KTTDSNRIKI
TNPDANNEST H
//