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Database: UniProt
Entry: D4IQE2_9BACT
LinkDB: D4IQE2_9BACT
Original site: D4IQE2_9BACT 
ID   D4IQE2_9BACT            Unreviewed;       636 AA.
AC   D4IQE2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily {ECO:0000313|EMBL:CBK65154.1};
GN   ORFNames=AL1_30630 {ECO:0000313|EMBL:CBK65154.1};
OS   Alistipes shahii WAL 8301.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK65154.1, ECO:0000313|Proteomes:UP000008794};
RN   [1] {ECO:0000313|EMBL:CBK65154.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK65154.1,
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:CBK65154.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK65154.1,
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; CBK65154.1; -; Genomic_DNA.
DR   RefSeq; WP_015547958.1; NZ_CP102253.1.
DR   AlphaFoldDB; D4IQE2; -.
DR   STRING; 717959.AL1_30630; -.
DR   KEGG; ash:AL1_30630; -.
DR   PATRIC; fig|717959.3.peg.1577; -.
DR   HOGENOM; CLU_014653_3_1_10; -.
DR   OrthoDB; 9777768at2; -.
DR   BioCyc; ASHA717959:AL1_RS14420-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: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; 3.30.1120.80; -; 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:UP000008794};
KW   Transferase {ECO:0000313|EMBL:CBK65154.1};
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..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          273..553
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         281
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         446
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         500
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         501
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   636 AA;  71647 MW;  EC0E5A6D5A0C7171 CRC64;
     MKRLLHTPLA LLVWRIALLY AALMLCRAAF WVYNAALLGP PEWSELGQLV AGSLKFDTAS
     VVYADGVFIL LSLLPLHLRE RRWYRGMLFW YYVIVNAVLI AAANLADTVY FRYTQKRFTA
     DEIFFADNDN SLQLAGKFMA ENWYLVLLWA GLVALLAWGY RRRTHEESVF SRGWAYYAGG
     TAVFALAAGL SVAGMRGGMT RMTRPITLSN AMLYTADSGK ANLILSNPFC ILRTIGSAGS
     VKYRKYFTPE ELPQRFTPVH QPADSAAVDL TGRNVMIFIM ESMSAEHSAF LHPELYADLP
     EKGFTPFLDS LMRNGLTFKR MYANGSRSIQ AMPSVLGSIP SFRTPFVLMP QSLGESRQLP
     AMLADKGYAT AFFCGSERGS MGFGAYARSA GVERLVSRED YEAKHGTRDF DGYWGIWDEE
     FLQFTGEELT AMPEPFFAAL FTLSSHHPFV VPEKYAATLP EGYTRIHKGV AYDDRAFRLF
     FQRFGGEEWF RRTIFVFVAD HVSSEKFAEE TRSYPGNMHI IGFIYTPDGA LRGEVGEITQ
     QLDIMPTLLG LTGNREPYFA FGRDVLNEPQ RPRWSVSYDG RFRALTGEGA IVLDDSDMNV
     QECPATPAAD SLAQNFRALV QQYYTHIEKK SYTAND
//
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