ID A0A0R2GTY5_9LACO Unreviewed; 697 AA.
AC A0A0R2GTY5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoglycerol transferase {ECO:0000313|EMBL:KRN43902.1};
GN ORFNames=IV41_GL001039 {ECO:0000313|EMBL:KRN43902.1};
OS Limosilactobacillus ingluviei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN43902.1, ECO:0000313|Proteomes:UP000051639};
RN [1] {ECO:0000313|EMBL:KRN43902.1, ECO:0000313|Proteomes:UP000051639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN43902.1,
RC ECO:0000313|Proteomes:UP000051639};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN43902.1}.
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DR EMBL; JQBA01000029; KRN43902.1; -; Genomic_DNA.
DR RefSeq; WP_056994689.1; NZ_JQBA01000029.1.
DR AlphaFoldDB; A0A0R2GTY5; -.
DR STRING; 1203076.GCA_000312405_01404; -.
DR PATRIC; fig|148604.4.peg.1076; -.
DR eggNOG; COG1368; Bacteria.
DR OrthoDB; 5901192at2; -.
DR Proteomes; UP000051639; 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:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 2.
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:UP000051639};
KW Transferase {ECO:0000313|EMBL:KRN43902.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..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..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..546
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 660..697
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 422
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 697 AA; 79077 MW; 7BC69A8A98FEDB6A CRC64;
MKTALQKVRA GLNTKLGFFA LSVLLFAIKS LWAYETKFNL GATTSVQQFL LAFNTLPSAI
ILLGIALYFR GRLSYWLMSI INALLSTWLF ANILYYREFS DFITFNVIKG SGSSSDNLGK
SLAQIIHPSD FMVYADVILI IIVLLAHWIR VDMRYFKRRY AATITAIGLL LFGANLGMAY
SDRSQLLTRT FDNNYIVKYL GLEFYTVYDG VKTTHNSAIK AEANKKDLAP VQRFLKQHYA
GPNATYYGTL KGKNIIVLHL ESFQQWLIDY KVDGKEVTPT INSLYHSSNT LAFDNFFNQV
GQGKTSDAEL MLEASLFGLP EGSAMSTNGT TNTFQAAPAI LDQKLGYSSA SFHGDVPSFW
NRDNAYKSFG YQYFFSKEYY PQVKDDVLGY GMKDKLFLKD TSYYLEQLPQ PFYAKLITVT
NHYPYIIDKK NTDFPALKTG DNTVDPYVQT AHYLDQSVKE LLDYLDKTGL RKNTVLVLYG
DHYGISNNHK PAIAKVLGKK NITSYDLAMW QKVPFMINAE GLQGGINHTY GGEIDVLPTL
EDLLGISSNK YLQFGQDLLS ADRNQIVPFR NGDWVTPKYT KYDGKYFYTK NGKPIAKPTK
AQQAKFDAIQ KYVTTDLGLS DKVINGDLLR FYHLPGFKDV NKKDYTYNLK KSLKKLKQAQ
KDKKTSLKTE NDDKSTFDDY TTDAPELKDD TTLKFPK
//
