ID A0A1L8MNB2_9STRE Unreviewed; 419 AA.
AC A0A1L8MNB2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000256|PIRNR:PIRNR016636};
DE EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR016636};
GN ORFNames=A9Q68_01425 {ECO:0000313|EMBL:OJF72232.1};
OS Streptococcus bovimastitidis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1856638 {ECO:0000313|EMBL:OJF72232.1, ECO:0000313|Proteomes:UP000182015};
RN [1] {ECO:0000313|EMBL:OJF72232.1, ECO:0000313|Proteomes:UP000182015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ1587 {ECO:0000313|EMBL:OJF72232.1,
RC ECO:0000313|Proteomes:UP000182015};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OJF72232.1}.
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DR EMBL; LZDD01000001; OJF72232.1; -; Genomic_DNA.
DR RefSeq; WP_071792886.1; NZ_LZDD01000001.1.
DR AlphaFoldDB; A0A1L8MNB2; -.
DR STRING; 1856638.A9Q68_01425; -.
DR OrthoDB; 9805788at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000182015; Unassembled WGS sequence.
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 19..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 419 AA; 49766 MW; B9A1DC5FA61B7A2F CRC64;
MIGMLSQIPY LDPYSNPSYF IYLIIALLPV ILGLFYQKRF HIYELIVTLV FVAMMFGQGH
TDQLKAFLLY IIWQTCSIFF YKWYRQKYDN FFVFALTLIL VIAPLFIVKI SPINPVHPNQ
SLFSFLGISY LTFKTIGMVM EMRDGLLKDF SLFTFLRFML FLPTFSSGPI DRYRRFQEDY
ETLPDRDSYL EMLNKAIKYI MIGFLYKFII SYYLGSVFLP IVEAKTIATG GYFNVYLILV
MYLYGLNLFF DFAGYSMFTI AISNLLGIKT PENFHLPFLA PNLKEFWNRW HMTLSFWFRD
FVFMRLVHFL IKHKVFKNRN VTSGFAYLVN MTIMGFWHGI TWYYIAYGIF HGLGLILTDA
WIRRKKTINC QRKQRGLAPL FTSKTYHYVS IVFTFHVVMV SLLLFSGFLD HFWIHPTHF
//