ID B7HKE1_BACC7 Unreviewed; 628 AA.
AC B7HKE1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Sulfatase {ECO:0000313|EMBL:ACJ81717.1};
DE EC=3.1.6.- {ECO:0000313|EMBL:ACJ81717.1};
GN OrderedLocusNames=BCAH187_A1576 {ECO:0000313|EMBL:ACJ81717.1};
OS Bacillus cereus (strain AH187).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ81717.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ81717.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ81717.1,
RC ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) 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 -!- SIMILARITY: Belongs to the LTA synthase family.
CC {ECO:0000256|ARBA:ARBA00009983, ECO:0000256|PIRNR:PIRNR005091}.
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DR EMBL; CP001177; ACJ81717.1; -; Genomic_DNA.
DR AlphaFoldDB; B7HKE1; -.
DR KEGG; bcr:BCAH187_A1576; -.
DR HOGENOM; CLU_021310_0_0_9; -.
DR Proteomes; UP000002214; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000313|EMBL:ACJ81717.1};
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 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..533
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 409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 468
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 469
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 628 AA; 72295 MW; E96BFF818C05CBCD CRC64;
MLQRLFPKLR FALVAVVLLW IKTYIVYKLA FDIKIDNFFE EFMLFMNPLA ALLLFFGFAL
FASKHRNRII VGISFILSFI LFGNAMFYGF YNDFVTFPVL FQTNNMADLG TSIKELFTYK
TLLLFADAII LMFLSRKFPS FCDKTPLSRS EKRTFFSGVT ALLALQIVVS VIYKPQMFSR
SFDRQTVVKN LGLYTYHLFD ITLQSKSSAE RVFASGDGFS EIKNYTDSKD KQVDKNLFGS
AKGKNVILIS MESTQSFVIN KKINGKEITP FLNEFIKDSF YFDNFYHQTG QGKTSDAEFI
VENSLYPLDR GSVFFTHATN EYTATPEQLK KYGYSSAVFH SNDKAFWNRD VMYPALGYDR
YFNLNDYVGT EQMSVGWGLK DKEFFEQSIP KLKSLPQPFY TKFITLTNHF PFLLNPEDQY
VDEFNSESGV VNRYFPTVRY TDEALKQFIK QLKAEGLYDN SVIVIYGDHY GISENHNAAM
AQFLGKDAIT PFDSMQLQRV PLIIHVPGQE GKVISKVSGQ IDIKPTLLHL LGIKTNKSVE
FGTDLFIKEE DPLMVMRDGS FVSEDYVYTK NMCYKRNTGE EADISLCQPN IEKAKTELKL
SDKLIYGDLL RFDPNNRYKT GTMITNFE
//
