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Database: UniProt
Entry: D4ILW5_9BACT
LinkDB: D4ILW5_9BACT
Original site: D4ILW5_9BACT 
ID   D4ILW5_9BACT            Unreviewed;       611 AA.
AC   D4ILW5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily {ECO:0000313|EMBL:CBK63927.1};
GN   ORFNames=AL1_14970 {ECO:0000313|EMBL:CBK63927.1};
OS   Alistipes shahii WAL 8301.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK63927.1, ECO:0000313|Proteomes:UP000008794};
RN   [1] {ECO:0000313|EMBL:CBK63927.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63927.1,
RC   ECO:0000313|Proteomes:UP000008794};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J.;
RT   "The genome sequence of Alistipes shahii WAL 8301.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK63927.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63927.1,
RC   ECO:0000313|Proteomes:UP000008794};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; FP929032; CBK63927.1; -; Genomic_DNA.
DR   RefSeq; WP_015546821.1; NZ_CP102253.1.
DR   AlphaFoldDB; D4ILW5; -.
DR   STRING; 717959.AL1_14970; -.
DR   KEGG; ash:AL1_14970; -.
DR   PATRIC; fig|717959.3.peg.3179; -.
DR   HOGENOM; CLU_014653_3_1_10; -.
DR   OrthoDB; 9777768at2; -.
DR   BioCyc; ASHA717959:AL1_RS06975-MONOMER; -.
DR   Proteomes; UP000008794; 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; 3.40.720.10; 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:UP000008794};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:CBK63927.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..611
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003058870"
FT   TRANSMEM        50..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          271..538
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        319
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         279
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         319
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         437
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         485
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         486
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   611 AA;  67753 MW;  BE3ED4A54FFCB6A0 CRC64;
     MRRKFAFLVT VFCATVLAMA VQKPVFMAWY AAEAAGAGFG GWMEVLWHGL TLDMTVAGYV
     TALPLLAVLL SLWVRIPERV WRGVLTAYFA LIAVVTAVIF AVDVALYEHW GFRIDATVLI
     YLSDPEEAMA SVDFWLGVRQ TLLAAAYAAP MLWAYCRILR IFDGRPVGWR LALPGSLVVV
     VLAGFDFLAI RGGLGASVAN VSKVYFSPVP FLNHAATNPV FSFLSSLGDR ADYAGEYPFF
     DEETRAAKFD ALRGNGPAAG PTERVLDTLR PNVVIVILES FARTVMDAEV DGEPVMPNMQ
     RLKREGVWFE NFFANSFRTD RGEVAILSGF PAQTRMSIMK LPAKSRNLPS VARSLAGEGY
     KTSFAYGGDL NFTNQASYMY ATGWQELIWQ KDLRFDAPAS DWGYDDRLMC DWFADRVIAL
     SESREPFLAG LLTLSSHTPF DVPYAKFDDR VLNAMAFSDD CVGKMIDRLK ASPAWENLLV
     VLVADHGYPY PRTLAYNEPL RHRIPMIWTG GAVARPRVVE DYASQIDIAA TLLAQLGVPH
     DDFDYSKDIF APTPPRKFAY YAFNDGFGVV DASGEAVWDA TGGRAVTETN PELLDVGRTM
     LQTTYVDIGR R
//
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