ID A0A1S9IHP3_9CLOT Unreviewed; 629 AA.
AC A0A1S9IHP3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OOO69839.1};
GN ORFNames=BS638_00160 {ECO:0000313|EMBL:OOO69839.1};
OS Clostridium tepidum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1962263 {ECO:0000313|EMBL:OOO69839.1, ECO:0000313|Proteomes:UP000190256};
RN [1] {ECO:0000313|EMBL:OOO69839.1, ECO:0000313|Proteomes:UP000190256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IEH 97212 {ECO:0000313|EMBL:OOO69839.1,
RC ECO:0000313|Proteomes:UP000190256};
RA Dobritsa A.P., Kutumbaka K.K., Werner K., Wiedmann M., Asmus A.,
RA Samadpour M.;
RT "Clostridium tepidum sp. nov., a close relative of Clostridium sporogenes
RT and Clostridium botulinum Group I.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OOO69839.1}.
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DR EMBL; MRAE01000001; OOO69839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9IHP3; -.
DR STRING; 1962263.BS637_06915; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000190256; 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: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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..539
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 304
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 304
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 629 AA; 72115 MW; BCC4EA4B09383D7C CRC64;
MSYILKVKNI IQKIAIRNLD IMLFLVLVSL KVMFYGKEIS PEFFSYKYIF LPVIASVGVL
LAIGYFLPKR KRSKFLYVIN IIISFIILAD LLYYRYYKDI ISIGAIRNAF LLGGVASSIT
SLFKLKDFLY FLDILVIFPF LKVYRNIPYK ENKAIIRIGI GSLILAGAIL LNGINIYRLS
VDQPGLLKTM SNRIYITKVL GNVNFHVIDA YQFTKNKINN SKKLPEEKEK EVVGNFQGKS
QVEGSKLKGV AKGKNLIVIQ VEALQQFVIN AKVEGQEITP NLNKWINRSM YFDNYFYQVA
AGNTSDAEFL SNNSLYPAAS GAAYYMYSGN QFKSLPSALQ DKGYYTAAMH GYKDGFWNRN
VMYKAQKFQD FYGESTYNID EQVGLGLSDK SFFNQSLEKM KTFKQPFYSF LVTLSSHFPY
DDVKGYGEFN VGKYEGSFLG NYLTGIHYTD AQLGMFLDNL EKEGYLDNSI VVIYGDHNAI
SKNYIQELYD FVGEKAPNDL KWYELQKVPM LIHFPKDEYK GVNHTYGGQI DLYPTIANLY
NLPREYMLGN DLLNVKEPKV TFRNGSFTDG NTFYISWTGE YYDIKTGEKI AETEELKTKK
QESSKDLQSS DELLNHNLIK KLESESKEN
//
