ID A8FBA6_BACP2 Unreviewed; 646 AA.
AC A8FBA6;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Glycerol phosphate lipoteichoic acid synthase {ECO:0000313|EMBL:ABV61523.1};
GN OrderedLocusNames=BPUM_0839 {ECO:0000313|EMBL:ABV61523.1};
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV61523.1, ECO:0000313|Proteomes:UP000001355};
RN [1] {ECO:0000313|EMBL:ABV61523.1, ECO:0000313|Proteomes:UP000001355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV61523.1,
RC ECO:0000313|Proteomes:UP000001355};
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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, ECO:0000256|PIRNR:PIRNR005091}.
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DR EMBL; CP000813; ABV61523.1; -; Genomic_DNA.
DR RefSeq; WP_012009359.1; NZ_VEIS01000034.1.
DR AlphaFoldDB; A8FBA6; -.
DR STRING; 315750.BPUM_0839; -.
DR KEGG; bpu:BPUM_0839; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_021310_0_0_9; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000001355; 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 ECO:0000256|PIRNR:PIRNR005091};
KW Manganese {ECO:0000256|PIRSR:PIRSR005091-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005091};
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 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..537
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 627..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 474
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 646 AA; 73462 MW; 8E7DF0D894BFF0BD CRC64;
MKKIFANKYS FFVLAVLLFW AKSYAAYKMD FNLGVKGSFQ EGLLLLNPFS SAIVFLGLAL
FLKGRKSAIV LIVIDFIMTA LLYANVAYYR FFDDFLTFST MKQAGNLGGG MTGGVLSSIK
PHDLLYFLDI IILIAIVIWR PEVKKFQMKK TFALLIVAAG VGLFFVNLHL AEKDRPELLT
RTFDHKYVVK YLGVYNYTIY DGVQSAQNAT QVANASSEDL TDVVNYTASH YAKPNAEYFG
KAKGKNIIKI HLESFQSFLI DYKLNGEEVT PFLNKLAHGK EDFTYFDNFF HQTGQGKTAD
AELMMDNSMF GLPEGAAFVT KGENTYQSLP AILDQKAGYT SAVLHGDYKS FWNRDTIYKH
MGYDQFFDAS YYNMDEENLV NMGLKDKPFF KESIPMLESM KKPFYAHLMT LTNHYPFNLD
EKDATIAKAT TGDKTVDNYF QTARYLDESL EQFFKDLKKS GMYKDSVILL YGDHNGISEN
HNRAMSEIQG KEITPYQNAQ NQRVPLMIRI PGKQGGVNHT YGGEVDVMPT LLHLQGIDSN
EYVNFGTDLF SKKHDQTVAF RNGNYVTPKY TLVDNTVYDT KTGKVVKQNK KTEAIKARVD
NQLSLSDKVL YRDLLRFHKL SDFKPVNPSD YFYGKSKDKE EDSSAK
//
