ID A0A0A1GZH6_9LACO Unreviewed; 700 AA.
AC A0A0A1GZH6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Glycerol phosphate lipoteichoic acid synthase {ECO:0000313|EMBL:BAP86399.1};
GN ORFNames=LOOC260_118930 {ECO:0000313|EMBL:BAP86399.1};
OS Paucilactobacillus hokkaidonensis JCM 18461.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP86399.1, ECO:0000313|Proteomes:UP000031620};
RN [1] {ECO:0000313|EMBL:BAP86399.1, ECO:0000313|Proteomes:UP000031620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LOOC260 {ECO:0000313|EMBL:BAP86399.1,
RC ECO:0000313|Proteomes:UP000031620};
RA Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.;
RT "Complete genome sequence and analysis of Lactobacillus hokkaidonensis
RT LOOC260T.";
RL Submitted (NOV-2014) 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; AP014680; BAP86399.1; -; Genomic_DNA.
DR RefSeq; WP_041094442.1; NZ_AP014680.1.
DR AlphaFoldDB; A0A0A1GZH6; -.
DR STRING; 1291742.LOOC260_118930; -.
DR KEGG; lho:LOOC260_118930; -.
DR HOGENOM; CLU_021310_0_0_9; -.
DR Proteomes; UP000031620; Chromosome.
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..545
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 657..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 305
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 480
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 481
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 700 AA; 78685 MW; 087B28F750182ED9 CRC64;
MKTVLQKVRG GLNTKLGFFL LTVVLFAIKS YVAYQNKFTL GVEGSIQKFL LAFNPFPAAI
LLIGIALYFR GRLSYWLMLL IDTIMSTWLF ANILYYREFS DFLSFSIMKG SGSVSNNLGK
SLMGILRPSD FLVYADVIIL ILLLAFHLIR IDPRYFKLRF AGIISVIAVV LFGFNLGMAE
SNRSGLLTRT FDSNYIVKYL GLEAYTVYDG VKTTQNNAVK AKASNSDIKP VLKFLKKNHA
DSNIQYKGVA KGKNVFIIHL ESLQQFMINY KWDGQEVTPN INKIYNSSDT IAFDNFFNQV
GQGKTADAEL MLENSLFGLS EGSAMVTDGT TNTFQAAPAI LDQKGYTTAS FHGDVPSFWN
RDNAYKSFGY QYFFSKSYFP KVKNYDAGYG IKDKLFMEDA ANYVQQLPQP FYAKLITVTN
HYPYILDKSN KSIKAWNTGD NTVDPYVQTA HYLDQSIGEF YNYLDKTGLR KNSMIVLYGD
HYGISNNHKP AIAKILGKKK VTNYDLAMFQ KVPFMIQMPG LKGGVNHTYG GEIDVLPTIE
NLLGIDSSKY VQFGQDLLSS NRNQIVSFRN GDFVSSKYTK YGGKTYNTTT GKELKNTTAT
QTSAIAKIQK YVTTELSLSD KVVNGDLLRF YKPKGFKKVD KSDYTYNLTK SLKRLKASQK
SNPTSVMAKN NGQSTLSDYS TDAPELKNID TSELVFPTVK
//
