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Database: UniProt
Entry: A0A168QFB4_9BACL
LinkDB: A0A168QFB4_9BACL
Original site: A0A168QFB4_9BACL 
ID   A0A168QFB4_9BACL        Unreviewed;       619 AA.
AC   A0A168QFB4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sulfatase {ECO:0000313|EMBL:OAB47720.1};
GN   ORFNames=PBAT_05125 {ECO:0000313|EMBL:OAB47720.1};
OS   Paenibacillus antarcticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB47720.1, ECO:0000313|Proteomes:UP000077355};
RN   [1] {ECO:0000313|EMBL:OAB47720.1, ECO:0000313|Proteomes:UP000077355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB47720.1,
RC   ECO:0000313|Proteomes:UP000077355};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PIRNR:PIRNR005091}.
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:OAB47720.1}.
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DR   EMBL; LVJI01000006; OAB47720.1; -; Genomic_DNA.
DR   RefSeq; WP_068647430.1; NZ_LVJI01000006.1.
DR   AlphaFoldDB; A0A168QFB4; -.
DR   Proteomes; UP000077355; 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   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   ECO:0000256|PIRNR:PIRNR005091};
KW   Manganese {ECO:0000256|PIRSR:PIRSR005091-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005091};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR005091-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077355};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          236..529
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         286
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         462
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         463
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   619 AA;  70985 MW;  110F97962E5DB6AC CRC64;
     MSWSSIKRLL KKPFVLFTII LLLKGYLAWA VTFGEVLPWK VLITEIPFIW LLFSLVEWFA
     SKRKLTWYMI INLLVTAIFF AVIMYYKYYG VIVTYHALEQ VNQVTAVSNS VFSLLAPYYL
     FIFTDIILFF ILSFRHTKFK QWKRHIAHKG SRRAVSLLFI FSLIVCLFNV LPNRASMNEI
     TQAQEMGILS YEAYTIFSKD KTELVPKDEI SQQSIDQLKG TTVPVNPAFS QAAKDKNIII
     IQLESFQNFL INLKIDGQEI TPNMNKLANS NFYFPNFYQQ VGQGNTSDAE FVVNTSFYIP
     SIGAATQNYP DKQLPSLPKL LKQHGYQSAT FHTNNVEFWN RRELYSALGF DKYYAQPFFE
     DEDVVFFGST DEVLYKKTAV KLQEMDQQPE PFYAQVISMT AHHPFTIPED KYKMTLPERY
     EGTFVGDYIR AQNYADYALG LFIEDLKKNG VWDNSLIVTY GDHMGLPMYS LERKDEQLMK
     EIYGHEYSYK DMLNIPLVIS GPGITSPSVF EQLGGQVDIL PTIANLAGAS LDSQIHFGQD
     LLNQNTNILP QRYYLPTGSF LSTKALFLSG SGYEDGTHYP LAGYEDSSGS ATKAEYEQAL
     QLLHLSDSYV NQLPDRKKN
//
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