ID A7GMQ9_BACCN Unreviewed; 388 AA.
AC A7GMQ9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000256|PIRNR:PIRNR016636};
DE EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR016636};
GN OrderedLocusNames=Bcer98_1091 {ECO:0000313|EMBL:ABS21417.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21417.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS21417.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- FUNCTION: O-acyltransferase that catalyzes D-alanylation of both
CC teichoic acid and lipoteichoic acid (LTA). D-alanylation of LTA plays
CC an important role in modulating the properties of the cell wall in
CC Gram-positive bacteria, influencing the net charge of the cell wall.
CC Catalyzes D-alanylation from DltC carrier protein.
CC {ECO:0000256|PIRNR:PIRNR016636}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000256|PIRNR:PIRNR016636}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR016636}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; CP000764; ABS21417.1; -; Genomic_DNA.
DR RefSeq; WP_011984170.1; NC_009674.1.
DR AlphaFoldDB; A7GMQ9; -.
DR STRING; 315749.Bcer98_1091; -.
DR GeneID; 56416677; -.
DR KEGG; bcy:Bcer98_1091; -.
DR eggNOG; COG1696; Bacteria.
DR HOGENOM; CLU_025255_2_0_9; -.
DR OrthoDB; 9805788at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR024024; DltB.
DR InterPro; IPR004299; MBOAT_fam.
DR NCBIfam; TIGR04091; LTA_dltB; 1.
DR PANTHER; PTHR13285; ACYLTRANSFERASE; 1.
DR PANTHER; PTHR13285:SF23; TEICHOIC ACID D-ALANYLTRANSFERASE; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
DR PIRSF; PIRSF500216; DltB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW 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 Transferase {ECO:0000256|ARBA:ARBA00022679, 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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 388 AA; 46347 MW; E9860F2C6E600837 CRC64;
MTAYGSFYFF VIVGILLIPT IIAGLKGKML RKYNAVLTLV MLAIIFSDKP KQAIMLAVFI
IWQYVLIRGY LHLRKQNNNT FMFCMAVILS ILPLILAKIA PFVPELKFVV FLGMSYVTFR
AVQMVFEVRD GLIKELSFFH FWEFVLFFPA ISTGPIDRYR RFQKDIQKPP SSEEYQQLLY
TGMNRIFQGF LYKFIIAYLI NQHLMEAAFA KQDTFLSNVI YMYSYSFYLF FDFAGYSAFV
IGVSYMMGIK TPENFNKPFI SRNIKDFWNR WHMSLSFWFR DFIYMRFVFF ATKKKLLKNR
YTISYIGAFL NFFIMGIWHI TGEHVYQYII YGLYHAALFI LFDIFERKNK KHKFWPNNKW
MHILAVVITF HFVCFGFLIF SGHLNRYF
//
