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Database: UniProt
Entry: A0A1G5I183_9FIRM
LinkDB: A0A1G5I183_9FIRM
Original site: A0A1G5I183_9FIRM 
ID   A0A1G5I183_9FIRM        Unreviewed;       500 AA.
AC   A0A1G5I183;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=D-alanyl-lipoteichoic acid acyltransferase DltB, MBOAT superfamily {ECO:0000313|EMBL:SCY69767.1};
GN   ORFNames=SAMN02910371_03450 {ECO:0000313|EMBL:SCY69767.1};
OS   Butyrivibrio sp. INlla14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCY69767.1, ECO:0000313|Proteomes:UP000199551};
RN   [1] {ECO:0000313|Proteomes:UP000199551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INlla14 {ECO:0000313|Proteomes:UP000199551};
RA   Varghese N., Submissions S.;
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; FMVS01000035; SCY69767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5I183; -.
DR   OrthoDB; 9805788at2; -.
DR   Proteomes; UP000199551; 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; 2.
DR   PIRSF; PIRSF016636; AlgI_DltB; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR016636,
KW   ECO:0000313|EMBL:SCY69767.1};
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:UP000199551};
KW   Transferase {ECO:0000256|PIRNR:PIRNR016636, ECO:0000313|EMBL:SCY69767.1};
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..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        392..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        470..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          170..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  57136 MW;  9A207C85873A5069 CRC64;
     MINFSDLTFI FRFLPVFIVA FYLTPCKYRK VTLLLGSLLF YAVGDLKMFP VLLGAVIINF
     LFSRALKGGG SKFLLGFAIC LDVLMLVEFK LLGQFVDSTL IPIGVSFFTF KMISFQIDNY
     RGKVSADAGF VDVAAYFTMF PQIVSGPIMR YEDYAKNPFL VRNSADAEEN FAQEQTQDQQ
     SETSVDNEGK EKDEILDLDT KEGMDKLENK HEIFSKIFSH IEDGLRFFVL GLGLKVLLAD
     HLAMLWNDIG TIGYESISTP LAWLGAVCYS MQLYFDFWGY SLMAAGIGVM LGFPFITNFD
     QPYSSKNVSE FYRRWHATLG SWFRDYIYFP MGGSRKGSFR TVLNLLTVWL ITGFWHGVTL
     NFIIWGLSIF VIILCERFIL SKCPKFINAI FGRINVLVLI PLTWVVFAIS NGNMLLDYFK
     RLFPFWGEGV SVNQGDFIKN IEIYGIILGF GLVLLIPQVY RFFEKHRKNP VFTIGLLVLF
     WACIYSLSNA AGNPFMYFKF
//
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