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Database: UniProt
Entry: A0A1Q5XW53_9BACL
LinkDB: A0A1Q5XW53_9BACL
Original site: A0A1Q5XW53_9BACL 
ID   A0A1Q5XW53_9BACL        Unreviewed;       628 AA.
AC   A0A1Q5XW53;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Sulfatase {ECO:0000313|EMBL:OKP98556.1};
GN   ORFNames=A3849_10435 {ECO:0000313|EMBL:OKP98556.1};
OS   Paenibacillus sp. P46E.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1349436 {ECO:0000313|EMBL:OKP98556.1, ECO:0000313|Proteomes:UP000185715};
RN   [1] {ECO:0000313|EMBL:OKP98556.1, ECO:0000313|Proteomes:UP000185715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P46E {ECO:0000313|EMBL:OKP98556.1,
RC   ECO:0000313|Proteomes:UP000185715};
RA   Ploux O.;
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:OKP98556.1}.
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DR   EMBL; LVYZ01000033; OKP98556.1; -; Genomic_DNA.
DR   RefSeq; WP_074111430.1; NZ_LVYZ01000033.1.
DR   AlphaFoldDB; A0A1Q5XW53; -.
DR   OrthoDB; 5901192at2; -.
DR   Proteomes; UP000185715; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          244..537
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         252
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         294
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         470
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         471
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   628 AA;  71359 MW;  AFD052103E628A6A CRC64;
     MQKEGEAVSS LNVKRWLIKP FVFFSILFIL KSFLAWGVIF GDLVSWKTLL TEIPFVWALF
     ALIERFASKR KLGYYMTVNL LVTAIFFAAI MYFKYYGVIV TYHAAEQVNQ VTAVRNSVFS
     LMDPYYLLIF ADIIVLGFYF FINKKGRTYK KDNINHRNGK LSHSLLFAVS LALCLFNILP
     NKASMNEIKK AQEMGILNYE AYTIFAKDKP ELVNASEITQ DAINKLKGID TAAVSPLQGI
     AKGKNLIIIQ LESFQSFLLG LKVDGQEITP NLNRLMENSL YFPNFYQMVG QGNTSDAEFV
     VNSSFYIPPQ GAATMAYVDK ELPSLPRLLQ NNGYQTATFH TNDVEFWNRG ELYSALGWEH
     YYDHKFFGDE DSFFFGPSDE ALYRKTSDKL KEMDTDSKPF YAQVISMSAH HPFTIPEEKY
     KMKLPERYEG TFVGDYVRSQ NYADYAFGQF VDELKANGVW DNSLIMVYGD HMGLPIYSLD
     HDDKELMTEI YGHDYEYANM LNIPLIVHDE GTIQPQTLDH VGGEVDIMPT AASLLGVSMD
     NNIHFGQDMT SQAYNLLPQR YYLPTGSFIA SSGLLIPGNS FEDNTQFTLA SGKKAPAGTE
     DEYNRALRLR QLSDSYVTQL PDKVKAAE
//
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