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Database: UniProt
Entry: D0R5P2_LACJF
LinkDB: D0R5P2_LACJF
Original site: D0R5P2_LACJF 
ID   D0R5P2_LACJF            Unreviewed;       689 AA.
AC   D0R5P2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Sulfatase N-terminal domain-containing protein {ECO:0000259|Pfam:PF00884};
GN   OrderedLocusNames=FI9785_1550 {ECO:0000313|EMBL:CAX67405.1};
OS   Lactobacillus johnsonii (strain FI9785).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=633699 {ECO:0000313|EMBL:CAX67405.1, ECO:0000313|Proteomes:UP000002627};
RN   [1] {ECO:0000313|EMBL:CAX67405.1, ECO:0000313|Proteomes:UP000002627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FI9785 {ECO:0000313|EMBL:CAX67405.1,
RC   ECO:0000313|Proteomes:UP000002627};
RX   PubMed=19767436; DOI=10.1128/JB.01182-09;
RA   Wegmann U., Overweg K., Horn N., Goesmann A., Narbad A., Gasson M.J.,
RA   Shearman C.;
RT   "Complete genome sequence of Lactobacillus johnsonii FI9785, a competitive
RT   exclusion agent against pathogens in poultry.";
RL   J. Bacteriol. 191:7142-7143(2009).
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}.
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DR   EMBL; FN298497; CAX67405.1; -; Genomic_DNA.
DR   RefSeq; WP_012846605.1; NC_013504.1.
DR   AlphaFoldDB; D0R5P2; -.
DR   KEGG; ljf:FI9785_1550; -.
DR   HOGENOM; CLU_021310_0_0_9; -.
DR   OMA; VSNHRPF; -.
DR   Proteomes; UP000002627; 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   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   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:UP000002627};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..546
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         305
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         422
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         481
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         482
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   689 AA;  78294 MW;  1779C691F4B1882E CRC64;
     MGRLKASYNW LTKTKLGFFT VVVVFFWIKT YLTYITKFNL GVVGSMQNFL LLINPLPTAI
     LLIGIGLFFK GRKSYWIMVI IDFLLSLWLF SNILYYREFS DFLSTSIIKT SGSTSDNLGK
     SIAGITKGTD FLVFLDVVII VLLIAFKVFK IDVRRLKLKV SFLIEGLAVV LIGTNLTMAQ
     KDRSGLLTRT FDNNYIVKYL GLNAFAVYDG VKTAQNNAIM AKANHSDLKT VQSYIKKNYI
     APNPEYYGVA KNKNVLVIHL ESFQQFLIDY KWHGKEVTPN LNKLYHANDT ISFDNFFNQV
     GQGKTSDAEM MLENSIFGLQ SGSAMSSYGT SNTFESAPAI LGQKAGYTSA VMHGGAGSFW
     NRDNAYKSFG YNYFMPLSYY QNKKGYYLGY GIKDKLFFDQ SIKYMEHLPQ PFYLKMITVT
     NHYPYDLDKK NQSIDKTDTG DKTVDGYVQT AHYLDQAIGE LMSYLKKSGL EKNTLIMLYG
     DHYGISGNHH KASAQLLDKD SFNNFDNLQF QRVPLMFHMP GLKGGINHTY GGEIDVRPTL
     FNLLGINDQN MIQFGHSLLA KNAPQIVAQR NGDFITPKYS KVEGSYYYTQ SGKRITHPSK
     EVKAQLASIS NTVTTELSLS DRVITGNLLR FYKPDGFEYV KRKNYSYKKS DSLKRLKKAE
     KKSKNSVWYQ NGKKTTQSYF KTDAPELKK
//
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