ID A0A0W7YGC8_9BACI Unreviewed; 631 AA.
AC A0A0W7YGC8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Sulfatase N-terminal domain-containing protein {ECO:0000259|Pfam:PF00884};
GN ORFNames=AK833_10285 {ECO:0000313|EMBL:KUF34101.1};
OS Lysinibacillus sp. F5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1700846 {ECO:0000313|EMBL:KUF34101.1, ECO:0000313|Proteomes:UP000053086};
RN [1] {ECO:0000313|EMBL:KUF34101.1, ECO:0000313|Proteomes:UP000053086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F5 {ECO:0000313|EMBL:KUF34101.1,
RC ECO:0000313|Proteomes:UP000053086};
RA Chan X.Y., Chan K.G., Hong K.W., Tan A., Chen J.W.;
RT "Draft Genome of marine Lysinibacillus sp. F5.";
RL Submitted (OCT-2015) 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}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000256|PIRSR:PIRSR600917-52}.
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:KUF34101.1}.
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DR EMBL; LKIE01000054; KUF34101.1; -; Genomic_DNA.
DR RefSeq; WP_058844154.1; NZ_LKIE01000054.1.
DR AlphaFoldDB; A0A0W7YGC8; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000053086; 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:SF1; LIPOTEICHOIC ACID SYNTHASE-LIKE YQGS; 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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..538
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT MOD_RES 64
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ SEQUENCE 631 AA; 72478 MW; 46F77EF3A10B5B86 CRC64;
MKSIKWPKHS FMILAIIATW IKTVIVYHTS FEMKIENAMQ QFILFINPLS FLLFTYGLSL
FFKSAKARNR YLITVSVILS IVLYGNVAFY RFYNDFITLP VLFQTSNFSD LGTSVAAIVE
PWDVLYFVDV AILILANKFL PKMKEAFKVN IEFRRAFFVL AVAISFLNLG LAETERPQLL
TRSFDRELLV KNIGTYNYHL YDIYIQTKSS AQRALADGSE LVEVNNYVRS NQAAVNPEMF
GKYKGRNLIV VSMESLQNFV INNDMNGHEI TPFLNSLTKD KDTYYFSNFY HQTGLGKTSD
SEFIVENSLF GLGRGAVFFT HGGNTYNSMA ERLGENGYFT NVMHPNNKSF WNRDIMYQSL
KINKFYDIDS YTVEEGQAVN WGMKDTPFLE QSAALMKDMP QPFYSRLITL TNHYPFTLDP
EDIMIPEYDS NSGTLNRYFQ TVRYMDEALK DFFQELKDQG VYDNSIIVMY GDHYGISENH
NKAMAQYLGK EQITPMDNAL LQEVPLFIHI PGSDDGKEMK EISGQMDLRP TILHLLGVET
SKDMQMGADL FSPEHEDFVV FRDGRFITDK YVYAGEACYD KATGEEIDGE PCQSYADRAT
MELENSDAII NGDLLRFYDE KTGNLKQDSV K
//
