ID A0A0K0GDL2_9FIRM Unreviewed; 629 AA.
AC A0A0K0GDL2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Sulfatase N-terminal domain-containing protein {ECO:0000259|Pfam:PF00884};
GN ORFNames=WH51_01305 {ECO:0000313|EMBL:KKE80633.1};
OS Bacilli bacterium VT-13-104.
OC Bacteria; Bacillota; Bacilli.
OX NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE80633.1, ECO:0000313|Proteomes:UP000034981};
RN [1] {ECO:0000313|Proteomes:UP000034981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA Tetz V., Tetz G.;
RT "Bacilli bacterium VT-13-104.";
RL Submitted (APR-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 -!- SIMILARITY: Belongs to the LTA synthase family.
CC {ECO:0000256|ARBA:ARBA00009983}.
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:KKE80633.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAZH01000005; KKE80633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0GDL2; -.
DR PATRIC; fig|1637974.4.peg.251; -.
DR Proteomes; UP000034981; 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 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:UP000034981};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..537
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 297
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 629 AA; 73073 MW; 9206EBC23DBAAE22 CRC64;
MNEKRPRIPL YITASLLFGI KTYIVYRFMF NIELDNSMQE FILFINPFVS AFVMFAISVW
FNKPSRQMKY IRYTGFIASF IVFANLVFYR QFTDFITIPQ LFMGSNMADL GSSILTLIKP
YDFLLFIDTV LIWVWSKRKE EFVKVSYQKR WKVFVLSLSL LLLAGNFLLA EMERPQLFTR
GFDREYLVKN IGLFNYHIYD IVQHSKAESQ RVFADGNELN DIKSFIDDNV RINEKSNMFG
AAEGKNVIWI NAESLQSFVI KNELNGEEVT PFLNSLIEDE DTYYFENFYE QTGQGKTSDS
EFLVENSMYP LSRGAVFFTH STNEYHATPE IIKDEGYNSA VLHANSGSFW NRFQMYDSIG
FDHFYDENSY EINPDNSVGW GLKDKPFFEQ SIKHLQSMDK PFYAKLITLT NHFPFELGEE
DRSIEPYHSN SNTLNNYFPA VRYMDEAIEE FFTLLESTDL YENSIIVIMG DHIGISANHN
KAMSMYLDKE EITPYDQVQL QRVPLLIHIP GDGNGKTIST VSGQIDIKPT ILSLLGIDTK
NDIYFGNDLF AKNRKSYIAL RNGDFISNEF IFTAGTCYNR ETGEIIEEDT NKGIEKVSSC
NEIRNNVETE LQHSDDLIYG DLLRFYDFD
//
