ID A0A161WHE0_9CLOT Unreviewed; 628 AA.
AC A0A161WHE0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Lipoteichoic acid synthase 2 {ECO:0000313|EMBL:KZL91105.1};
GN Name=ltaS2_2 {ECO:0000313|EMBL:KZL91105.1};
GN ORFNames=CLMAG_28630 {ECO:0000313|EMBL:KZL91105.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL91105.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL91105.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL91105.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-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:KZL91105.1}.
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DR EMBL; LWAE01000003; KZL91105.1; -; Genomic_DNA.
DR RefSeq; WP_066623227.1; NZ_LWAE01000003.1.
DR AlphaFoldDB; A0A161WHE0; -.
DR STRING; 1121326.CLMAG_28630; -.
DR PATRIC; fig|1121326.3.peg.2881; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000076603; 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 Reference proteome {ECO:0000313|Proteomes:UP000076603};
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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 254..541
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 628 AA; 71984 MW; 85881D3F5FA6608D CRC64;
MSIDMIKQSR VTHFLIRNLD IILFAAIIFF KLMLYAKQIS PEYLYMGVTH PVFASVLILA
SFSMLFEHKT RMNFLYTINL IIGLVLISDI MYYKYFKDVT TVAALRNIKL LSGVSSSVTS
LIDIKDFIYV IDTIILFPFL KRYKNAKRKY NSTAVNKIVF FLLIFVTGIS IDAKSVAAIA
KEQPTLLSAM SNRIYLTKMI GNLNFHAVDA YNYISTNVKN SKKLSSERVT EIKSYLDDNN
QITGSNLRGE AQGKNLIVIQ VEALQQFAIN KKVDGKEITP NLNKWINKSL YFDNYFYQVA
GGNTSDAEFM SNNSLYPAAS GAAYYTYSGN QYNSLASQLK NSDYYTAALH GYSEGFWNRN
VMYKSESFDN FYGEHSFNVN EEVGLGLSDK SFLDQSIEKL KTFKEPYYSF LVTLSSHFPY
DDSQGYGDFN VGQYENSILG NYLKGIHYTD EQLGMFLDKL DQEGITKNSL IVIYGDHFAI
PKENINELYS FENVNNPDDL KWFQYQKVPL IIHFPEDENK GVNHTYGGQM DLYPTLANLF
NLPRDYMFGK DLLNSNSNKV LFRSGSFTDG NAFYVSWTNT YYNIKTGNII PETDELKKKK
EEYTRELGYS DDMLNHNLIK SFEGDKSK
//
