ID A0A089JYE7_9BACL Unreviewed; 630 AA.
AC A0A089JYE7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Sulfatase {ECO:0000313|EMBL:AIQ25859.1};
GN ORFNames=H70737_25190 {ECO:0000313|EMBL:AIQ25859.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ25859.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ25859.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ25859.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009279; AIQ25859.1; -; Genomic_DNA.
DR RefSeq; WP_042191491.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089JYE7; -.
DR KEGG; paej:H70737_25190; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_1_1_9; -.
DR Proteomes; UP000029519; Chromosome.
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:UP000029519};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..540
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 475
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 630 AA; 70924 MW; 4559CF6CBA1B447F CRC64;
MKKQGPDRAH FFIVVILLWL KLLLLRVLFF DRIAWEWIAA DVAPVLFIMG ILTVITPSRV
RTTVYWIFNG FLSLLLFAAA VYFNHFGSVP TYLALSEINQ VFQVKASVES TIKSIDYLFF
VDFVIFAIYG LIRRWKQGKT YPRERFSSRK TGFVHVVVIL VSIIGGFSLS AYSVHSARGI
TNELVQAETA GFLNYEVVAA IKINEDNNLI GTGDIKDTIA KVDALQSSYP YSDKPAGTTP
DYFGSQKGKN VIVLQLEAFQ NFPLHQSLDG QELTPVMNKL ADEGFYFPHV YQQIGPGNTS
DAEFMSNTSI YPIGTLAMST GFGDRELPSL PRLLRDKGYE AYTFHVNKVG FWNRNELYPA
LGFNGYYDKD YFTNDHFNAF GASDEQLYIT GVEKLTELKK KGTPFYAQMV TASSHHPFKI
PDSFKKITVP DNLKDTMLGD YLTAINYTDY AIGTLIEGLK ENGLWDNTVL VMYGDHFGLQ
PQDVPPEQVE SALGVPYDSR ISRFNIPLIV RVPGMEQGKV VERTGGQLDI LPTIANLMGV
SLQQEGYTAF GHDLLNIDRN VLGMRYYLPS GSFFNDDILY VPGKGFADGE AVSLDTLKPV
TDFSKYQSDY EYVLKLMNLS DEYVKLLPQR
//
