ID A0A1I0YU55_9FIRM Unreviewed; 529 AA.
AC A0A1I0YU55;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=D-alanyl-lipoteichoic acid acyltransferase DltB, MBOAT superfamily {ECO:0000313|EMBL:SFB16742.1};
GN ORFNames=SAMN05216249_11162 {ECO:0000313|EMBL:SFB16742.1};
OS Acetitomaculum ruminis DSM 5522.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetitomaculum.
OX NCBI_TaxID=1120918 {ECO:0000313|EMBL:SFB16742.1, ECO:0000313|Proteomes:UP000198838};
RN [1] {ECO:0000313|EMBL:SFB16742.1, ECO:0000313|Proteomes:UP000198838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5522 {ECO:0000313|EMBL:SFB16742.1,
RC ECO:0000313|Proteomes:UP000198838};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010323, ECO:0000256|PIRNR:PIRNR016636}.
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DR EMBL; FOJY01000011; SFB16742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0YU55; -.
DR STRING; 1120918.SAMN05216249_11162; -.
DR OrthoDB; 9805788at2; -.
DR Proteomes; UP000198838; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR028362; AlgI.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13285; ACYLTRANSFERASE; 1.
DR PANTHER; PTHR13285:SF18; PROTEIN-CYSTEINE N-PALMITOYLTRANSFERASE RASP; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF500217; AlgI; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|PIRNR:PIRNR016636,
KW ECO:0000313|EMBL:SFB16742.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR016636};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR016636};
KW Reference proteome {ECO:0000313|Proteomes:UP000198838};
KW Transferase {ECO:0000256|PIRNR:PIRNR016636, ECO:0000313|EMBL:SFB16742.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 529 AA; 61113 MW; 4B9F4C969F830114 CRC64;
MQYNSYMYLF AFLIPVVILY YIIPIKYRWG VLLTASIVFY LFSSKYLIVS ILFTSLLVYL
AAKNIEDRNL KFKEIKKSLE KPERKLLKEK NEKKNNLVCG LVAIISLGIL FFSKYLNFAG
NIANSFCRLL NINMQFETVH LLMPLGISFY TLSAIAYVID VKRGVCEAEK KPLKIFLFLS
FFPTVTEGPI ERYKNVGKML STGHSFDYKT FCFGLQLMMW GLFKKIVVAD NLNRYVMVVF
RDYKNFGNWV IILMVLVYTL ELYADFSGCI DIARGSAELF GIELSENFKQ PFVSKTVNEF
WQRWNITLGS FLRDYVFYPV SLSTGFQNLS KKSKKVFNNY YATTVPMIFA LFMVWLCNGL
WHGSEVKYVV YGLYYYAILT LGLLLEPLFK KIFESLNINR ESKGYQRCQI ARTFILVNIG
MMIFNSKDIA SAKEMFFAMF KPSAISNIPQ ELLNTGMQSP AMVLLFIIPV IIFAFVGHFH
EQGISIREYL AQKPLFYRWS FYLAGVAVII SLGAYGVGFK GADFIYAQF
//