ID A0A0X7BFN3_9FLAO Unreviewed; 478 AA.
AC A0A0X7BFN3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=D-alanyl-lipoteichoic acid biosynthesis protein DltB {ECO:0000313|EMBL:KVV15881.1};
GN ORFNames=AP058_00497 {ECO:0000313|EMBL:KVV15881.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV15881.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV15881.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV15881.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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}.
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:KVV15881.1}.
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DR EMBL; LLWK01000029; KVV15881.1; -; Genomic_DNA.
DR RefSeq; WP_066306568.1; NZ_LLWK01000029.1.
DR AlphaFoldDB; A0A0X7BFN3; -.
DR STRING; 1729581.AP058_00497; -.
DR PATRIC; fig|1729581.3.peg.530; -.
DR OrthoDB; 9805788at2; -.
DR Proteomes; UP000059935; 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 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:UP000059935};
KW Transferase {ECO:0000256|PIRNR:PIRNR016636};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 478 AA; 55934 MW; A83BD858F3FBBA7A CRC64;
MLFNSFPFAI FVPVIFVLYW FVFQKSLKAQ NILILAASYF FYSCWDWRFL FLLLFSTALD
YFSGLQLEKN SNTTVRKFWF YGTIGINLSF LGVFKYFDFF VLSFQNLFLK MGYAIDVFTL
NIILPVGISF YTFHGLSYVI DVYKKRIRAE KNFVEYAVFV SYFPLLVAGP IERATHLLPQ
IKAKRNFNYD QAVSGLYQIL WGLFKKIVIA DNCARFANEI FNDPSQYSGS TLVAGALFFT
FQIYGDFSGY SDIALGVSKL FGIELLKNFA FPYFSRDIAE FWRRWHISLS SWFKDYLYIP
LGGSKGGKAM QIRNTFIIFL VSGFWHGANW TFLIWGFLNA LYFIPLLLTN KNRINLDIIA
QDRLLPSMRE SLQMFTTFAL TVFAWVFFRA DSVSSAFHFI NGIFSKSLIS LPQIRPTFLI
ILIIFFIVVE WLGRQGNFAL DNFKKYGSRA FRWTFIILIL TLLFIFGKEE QQFIYFQF
//
