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Database: UniProt
Entry: J3JBP8_9LACO
LinkDB: J3JBP8_9LACO
Original site: J3JBP8_9LACO 
ID   J3JBP8_9LACO            Unreviewed;       676 AA.
AC   J3JBP8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Alkaline phosphatase superfamily protein {ECO:0000313|EMBL:EJN55912.1};
GN   ORFNames=A11Y_117536 {ECO:0000313|EMBL:EJN55912.1};
OS   Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN55912.1, ECO:0000313|Proteomes:UP000007271};
RN   [1] {ECO:0000313|EMBL:EJN55912.1, ECO:0000313|Proteomes:UP000007271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA   Rodriguez J.M.;
RT   "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL   Submitted (MAY-2012) 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:EJN55912.1}.
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DR   EMBL; AKFP01000027; EJN55912.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3JBP8; -.
DR   STRING; 1185325.A11Y_117536; -.
DR   PATRIC; fig|1185325.3.peg.1291; -.
DR   Proteomes; UP000007271; 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:UP000007271};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          204..500
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   REGION          623..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT   BINDING         212
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         256
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT   BINDING         432
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ   SEQUENCE   676 AA;  76037 MW;  804BDF6EB5C7163E CRC64;
     MWLNPLATTL LVFGLALYIQ RPFWRYFGLM ILATANTALL YFNVIYYRQF TDFMTINTIL
     GYSKVSEGLS GSSLALARPY DVLYWLDLII LVVLLIARLI KIDQRPVPRR FPFAITSVAV
     LLFSINLTLG EANRPQLLTR TFDRNYIVKY LGLDAYTVYD AVKTAQNNQT RASANGSDLT
     NVLSFINQHY AAPNPKMYGI AKGRNVIIIH LESFQQFLID YKVDGREVTP FLNSLYHDDQ
     TYAFSNFFHQ VGQGKTSDAE NMLETSVYGL PQGSVFTALG SDNTFQAAPA ILQQKAGYSS
     AVFHGNVGSF WNRDNVYKNM GYQNFFDASY FNTTGDRSEQ YGLKDKLLFH DSVKYLEQLQ
     QPFYAKFITV TNHFPFPLDS EDTDFPLPTT DDKAVNNYFG TAHYLDQALQ EFFAYLKASG
     LYDNSMIVLY GDHYGLSNSD NLSLAELLGK SSDTWNDYDN AQLQRVPLMI HIPGQHDGGI
     QKQYGGEIDV LPTIEHLLGI DNKGYIQFGT DLFSPQHDQV VAFRNTNFVT PSHTVIDGTI
     YNNNGDEITH PSTELQATIK RQQTKVQNEL QLSDAVNNKN LLRFYTPTGF KPVDPESYNY
     KNDFASLKLA GEKLGKLSTS LYAKNGDRTT SNHYKTDAAE LSDSSSDNDS ANNSDSDSNS
     NSMDYSSAMS SMTGQN
//
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