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Database: UniProt
Entry: A0A1L8MNB2_9STRE
LinkDB: A0A1L8MNB2_9STRE
Original site: A0A1L8MNB2_9STRE 
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
//
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