ID M1MHC6_9CLOT Unreviewed; 605 AA.
AC M1MHC6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Phosphoglycerol transferase family protein, alkaline phosphatase superfamily {ECO:0000313|EMBL:AGF57309.1};
GN ORFNames=Cspa_c35480 {ECO:0000313|EMBL:AGF57309.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF57309.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF57309.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) 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}.
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DR EMBL; CP004121; AGF57309.1; -; Genomic_DNA.
DR RefSeq; WP_015393625.1; NZ_AOIF01000055.1.
DR AlphaFoldDB; M1MHC6; -.
DR STRING; 36745.CLSAP_33220; -.
DR KEGG; csr:Cspa_c35480; -.
DR PATRIC; fig|931276.5.peg.3574; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_1_0_9; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000011728; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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:UP000011728};
KW Transferase {ECO:0000313|EMBL:AGF57309.1};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 258..543
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 308
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 421
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 605 AA; 70052 MW; 4158DA0749585CEB CRC64;
MKQRLKSIFI NNWLFLFMVV VLQYKSIILL SMLRTQDSSS INLGDIYFGT PVKWAHIAII
FLICSPILLF KEKGRLRTAA IIDLLVTILF VADIWYYRAN GTFLSVRYMT HSEIFNPIGK
NLLNFRLVDL SFIIDFVILF LICKFAKIKA SDRNSKLQFR IIKGFSVFLI SAVVVGLGHY
FIDIKRIDPS RNLFSQSWAP FQTFSDMSPL GYHGFDINFY QDKNKKLSNE DEDKIKNWME
NNKENLPDNQ YKGIFKGKNL IAIQVESMEN FVINQKVYGQ EITPNLNKLL GSSIYFNNIY
EQNNSGTSSD CDLLVNSSIF PIREGKTVFS YPWTTFNSLQ KNLENEGYKT ISTHAEVPGN
WNWAELHKSF KADEIWDIGQ YNVDEKIGLG LSDESYLRQI SQKLKNQKEP FYAFMTTLTS
HGPFEMPDNK KYLNLPKELD ENMLGAYFQS VRYTDEAIGK FIAELDKNNQ LDNTVIMIYG
DHCGVHKFYE DDIKNSPLEG DWWKDNHKKI PYIIYSKGSQ PEVISKAGGQ SDFLPTILYM
LGYDRKAFED SSMGRVLVNT ERDATILNDG QIMGIPKDEK ELNHLKETFD IADTIIEKNY
FKNKY
//
