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Database: UniProt
Entry: I4ZAQ3_9BACT
LinkDB: I4ZAQ3_9BACT
Original site: I4ZAQ3_9BACT 
ID   I4ZAQ3_9BACT            Unreviewed;       582 AA.
AC   I4ZAQ3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Phosphoglycerol transferase family protein, alkaline phosphatase superfamily {ECO:0000313|EMBL:EIM33295.1};
GN   ORFNames=PrebiDRAFT_1601 {ECO:0000313|EMBL:EIM33295.1};
OS   Prevotella bivia DSM 20514.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM33295.1, ECO:0000313|Proteomes:UP000002786};
RN   [1] {ECO:0000313|EMBL:EIM33295.1, ECO:0000313|Proteomes:UP000002786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM33295.1,
RC   ECO:0000313|Proteomes:UP000002786};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL   Submitted (FEB-2012) 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; JH660660; EIM33295.1; -; Genomic_DNA.
DR   RefSeq; WP_004337489.1; NZ_JH660660.1.
DR   AlphaFoldDB; I4ZAQ3; -.
DR   GeneID; 78531544; -.
DR   HOGENOM; CLU_014653_3_1_10; -.
DR   Proteomes; UP000002786; 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: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:UP000002786};
KW   Transferase {ECO:0000313|EMBL:EIM33295.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          257..504
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         250
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         452
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         453
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   582 AA;  66733 MW;  B0F6FE765A8245AB CRC64;
     MLFNYGMFKD SGVADYVQVM WHGISLDLSM AGYFLLLPCL LTIVSVWISN KAVLWLWLWR
     MAIAFSALLF SFSFCLNLAL YPYWKFPLDT TPLFYFLSSP ADAFASVNIL TVILGFVVSF
     ALTGAVYTLF VHFIPKFHTA NLRCKMLQTL VVVLFMVVLI IPIRGGVSVS VTNIGKVYFS
     TNMKLNHAAV NPLFSLMESY SKEEDFSKQY RFMEHSEMER IFKTMVSTKS TDTKALLNTD
     KPDIYLFILE SFSTKLMQTE ATPQLNQLKK EGIFFENLYA NSFRTDRGVV AVLSGYPAQP
     TTSIMKFTKK ASALPSIANV LKQHHYRLKY YYGGDANFTN MRSYLTSQGF VNIVSDVDFP
     LKYRLSKWGV PDEYVFERLI DDIKVRKQSD KQPTFQVLQT SSSHEPFDVP YYRLKNKVLN
     AFAYTDHCIG NFVSYLKKSG RWNRSLIILV PDHLGCYPED ISSFTLERYQ IPMLWLGGAI
     KNPQRVSTYG SQHDIAATLL AQLGLSHQQF LFSKDMLDAH STHFAFFTFP DLWGIATPDH
     KLIYDNTSNK LILKQGEETD LYTKKGKAYL QRLYDDLSER GE
//
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