ID A0A136M1B1_9BACT Unreviewed; 609 AA.
AC A0A136M1B1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Sulfatase {ECO:0000313|EMBL:KXK27667.1};
GN ORFNames=UZ12_BCD005001261 {ECO:0000313|EMBL:KXK27667.1};
OS Bacteroidetes bacterium OLB12.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK27667.1, ECO:0000313|Proteomes:UP000070129};
RN [1] {ECO:0000313|EMBL:KXK27667.1, ECO:0000313|Proteomes:UP000070129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK27667.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-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 -!- 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:KXK27667.1}.
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DR EMBL; LNFR01000050; KXK27667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136M1B1; -.
DR STRING; 1619897.UZ12_BCD005001261; -.
DR PATRIC; fig|1619897.3.peg.1370; -.
DR Proteomes; UP000070129; 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; 3.30.1120.80; -; 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 4: Predicted;
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 264..533
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 312
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 312
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 427
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 609 AA; 68921 MW; 5159C181890A0F4E CRC64;
MRYRLRFFGL LALYWMAYFT LGRVLFLLYL LPQTNSLSLQ EITMPLLLGL RMDAAMTGYW
LLLPGLLFVA SAFTSNRFTF YATGIITIML LLISTILVVT DLELYKHWGF RINSTPLMYL
ESEAISSVNS GVLVGLILIF AALFSSFIFI YSRWLAPQLL TLPPIKKKHA LTWLVITTAL
LIPIRSSFTV APLNTGVVYF HKTKSFPNHA GINPVWNFFR SVSKSKAVKY PGDFYQAGNL
DAEFKSLMQT SETQFAIDST IHHPNVLLII LEGFTSKIIE PLGGLPNITP EFNALISEGM
LFENFYASGD RTDKGLVSIL SAYVAQPRTS IIKFPEKTQH LPFLSKELER NGYATSFIYG
GDVGFANMES YLTIAGFGSI TDEDEFDSNL NDSKWGVADH YVFTKMLREL NAAPNPFFKV
MLSLSSHEPF EVPMETVIPG KDEGSMFLNA CYYTDRSLGE FIRQAKQQPW WKNTLVIVTA
DHGHRFPDLL ELKDKSRFKI PMLWLGGVIT RPGTRIGTFA SQTDIANTLL AQLRIQPQSE
FLFSKNILAR SVNPFAVYVF NNGFGYVSAT HESIYDFDIK NYVSQTGNEN ELTNGQIYMQ
TLFNDYNRK
//