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Database: UniProt
Entry: A0A108U892_9GAMM
LinkDB: A0A108U892_9GAMM
Original site: A0A108U892_9GAMM 
ID   A0A108U892_9GAMM        Unreviewed;       652 AA.
AC   A0A108U892;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Phosphoglycerol transferase I {ECO:0000313|EMBL:KWS04391.1};
DE            EC=2.7.8.20 {ECO:0000313|EMBL:KWS04391.1};
GN   ORFNames=AZ78_1940 {ECO:0000313|EMBL:KWS04391.1};
OS   Lysobacter capsici AZ78.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS04391.1, ECO:0000313|Proteomes:UP000023435};
RN   [1] {ECO:0000313|EMBL:KWS04391.1, ECO:0000313|Proteomes:UP000023435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ78 {ECO:0000313|EMBL:KWS04391.1,
RC   ECO:0000313|Proteomes:UP000023435};
RX   PubMed=24762937;
RA   Puopolo G., Sonego P., Engelen K., Pertot I.;
RT   "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT   to Plant-Pathogenic Oomycetes.";
RL   Genome Announc. 2:0-0(2014).
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   -!- 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:KWS04391.1}.
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DR   EMBL; JAJA02000001; KWS04391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A108U892; -.
DR   OrthoDB; 9760224at2; -.
DR   Proteomes; UP000023435; 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: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   Transferase {ECO:0000313|EMBL:KWS04391.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          287..557
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         506
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         507
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   652 AA;  72170 MW;  652E48A312E7CE7F CRC64;
     MRVIKDYLAR VVPFLCCFGI GLAVLSLSRL GLVLWQADAV NDADAWSRVL LQGIRVDTAT
     LCMLLGIASA LYLLLPVSVA RHALVRTTMA AWLALSLTVL VVLELATPTF MQEYGLRPNR
     LFLEYLIYPR EVVSTLAKGH LVGAALALVL GAIAGWFAWR FANRMLRASA QASPHWSARL
     PFAALLICLA ALGIRSTLGH RPMNPAMMAF SSNATVNTLP LNSFYTLAYA ARDWLRHDPG
     ARIYGGAADA EVVKAVTDGM QLPPEAFIDP KLPTLARRPP AYTGKPRNLV IVLEESLGAQ
     FVGHLGGRPL TPNIDRLAAQ GWAFDRLYAT GTRSVRGIEA VLTGFTPTPS QAVVKQPLSQ
     QNFFTLAEVL RRRGYDTTFY YGGESHFDNM RGFFLSNGFR GVIEQKDYAH PAFTGSWGVS
     DEDLFDRAHQ EFARMHQAGK PFFGFVFSSS NHDPFEFPSN RIELYEQPQA TRNNAAKYAD
     YAVGEFFRKA MASDYWKDTI FLIVADHDSR AFGRDLVPID NFHIPGVILG GAVAPALDKR
     IVSQIDLPPT LLSLIGIDTP TPMSGHDLNQ RDRFQPGRAM MQYDKNFAWM SGKDVIVLQP
     GQPPRQFTYT PGERMTPAPS VDPELAKTAH LQALWGTLAY ERGWHRLPAK SD
//
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