ID A0A1G9YH27_9BACI Unreviewed; 647 AA.
AC A0A1G9YH27;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Phosphoglycerol transferase MdoB {ECO:0000313|EMBL:SDN07773.1};
GN ORFNames=SAMN05216244_4142 {ECO:0000313|EMBL:SDN07773.1};
OS Sediminibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=482461 {ECO:0000313|EMBL:SDN07773.1, ECO:0000313|Proteomes:UP000182347};
RN [1] {ECO:0000313|EMBL:SDN07773.1, ECO:0000313|Proteomes:UP000182347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6199 {ECO:0000313|EMBL:SDN07773.1,
RC ECO:0000313|Proteomes:UP000182347};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNHF01000009; SDN07773.1; -; Genomic_DNA.
DR RefSeq; WP_074601105.1; NZ_FNHF01000009.1.
DR AlphaFoldDB; A0A1G9YH27; -.
DR STRING; 482461.SAMN05216244_4142; -.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000182347; 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 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:SF1; LIPOTEICHOIC ACID SYNTHASE-LIKE YQGS; 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 Transferase {ECO:0000313|EMBL:SDN07773.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..532
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-1"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-2"
FT BINDING 468
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
FT BINDING 469
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR005091-3"
SQ SEQUENCE 647 AA; 75168 MW; F1693059F4CD947A CRC64;
MSKKLFNIPL YIIATVLFGL KTYIVYRFIF EISLDNWMQE FILFVNPFAS AFLVFALSVW
FKERRQMKFL RYAALIGTLI IYFNLIFYRN FTDFITIPVL FQGSNAADLG SSFMSLVHIP
DLLLFLDVAI IWVLSRKYPS VISAGYHKRG KTLALSVSLL FLLFNYTLAE IERPQLLQRT
FDREYLVKNI GLFNYHIYDA VLQSKTKAQR VFADGNEMPE ITEYVDEHVQ NEEKSDMFGV
AKGKNVIFIS LESVQNFVIN NKVNGEEITP FLNDLIDESY YFENFYHQTE QGKTSDSEFL
IENSLYPLSR GAVFFTHGQN EYHASPEILG ENGYFTSVFH ANNKSFWNRD VMYDSLGYDK
FFDVDSYEVT EDNSIGWGLK DKPFFEQSMK YLQSQQQPFY SKFITLTNHY PFDLEEEDAS
IDKYDSNSKT LNQYFPTVRY TDEAVEQFFK DLKESGLYEN SVIVLMGDHY GISEFHNKAM
GQYLGKEITP YEHIQLQRVP LFIHIPGEEG GVISEIAGQI DVKPTILSLL GIETDDDITF
GTDLFAKDRK EFIALRNGDY ISDDYIYTKG QCYDRKTGEL LESEPTGLEQ KQEDTAEGLC
EPIKEKVDKE LSYSDKLIYG DLFRFYDFND EEDGQDEQND QSDQVEQ
//
