ID Q1GAY2_LACDA Unreviewed; 740 AA.
AC Q1GAY2;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Putative phosphoglycerol transferase {ECO:0000313|EMBL:CAI97519.1};
GN OrderedLocusNames=Ldb0690 {ECO:0000313|EMBL:CAI97519.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97519.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI97519.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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}.
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DR EMBL; CR954253; CAI97519.1; -; Genomic_DNA.
DR RefSeq; WP_011543755.1; NZ_JQAV01000001.1.
DR AlphaFoldDB; Q1GAY2; -.
DR STRING; 390333.Ldb0690; -.
DR KEGG; ldb:Ldb0690; -.
DR PATRIC; fig|390333.13.peg.109; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_0_0_9; -.
DR BioCyc; LDEL390333:LDB_RS02995-MONOMER; -.
DR Proteomes; UP000001259; 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: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:UP000001259};
KW Transferase {ECO:0000313|EMBL:CAI97519.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..549
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 695..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 304
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 482
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 483
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 740 AA; 82798 MW; 59FDF8A6C47A1C82 CRC64;
MKHSKFLGKF QSRTGFLTLL VICYWLKYLF VAYCDFNLGL ANPLQHIIMW FSPLGTSIIL
ISLGFYFSKP LASYIAMLAL DFANTALLFA NVLYYRQFTD FITVKTMANL SKVSQGLGKS
SAALLAPSDI FIWLDLIVIV ILLAVKVIKI DQRSYGFSRT FAITSFGFFV LGLNMMVAEC
NRPRLLKNTF DRTYVVKYLG IDTFTVYDAI KNESSSTVTK NASTSELNKI INFTQQNYAP
ANSEYFGAEK GENVIIIHLE SFQQFLIGMK VNGKEVTPFL NSLYKNKHTL SYSNFYHQVG
LGRTSDAENM LETSTYGISD GSLFTSLGSS NTFQASPQIL RANSNYTSAV FHGNVGSFWN
RNDVYKNMGY NYFFDKNYFS QESGDSSGYG LKDKLFFAES VKYLERMQQP FYAKFITVTN
HTPFELATAD QDPNFKTSST SDVTINNYFL TAHYLDQALK EFFTYLKKSG LYEKSMIVIY
GDHYGLSNEE YTTLAPLIGK NPNDWSSYNT AQMQKVPFMI HASNLKGGIK STLAGEIDVL
PTILHLLGIS SKQYVQFGTD MLSAKHKQIV VFRNGTVISP KYVLIGGKTS KGNVYDASGK
LLTKLTKKQK AEVKKLAAYG KNSLAYSDTL NNKNLLRYYT PKGFSPVIPS DYNYSTNYQQ
MMDLIEQLGK QSTALISQKG DTSKLYKTDA SQLAKRQSEI TQIPESILSS SSSMNESMTS
SSSSSSASSS SSKASSKKTK
//
