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Database: UniProt
Entry: A0A0R1ZGA2_9LACO
LinkDB: A0A0R1ZGA2_9LACO
Original site: A0A0R1ZGA2_9LACO 
ID   A0A0R1ZGA2_9LACO        Unreviewed;       399 AA.
AC   A0A0R1ZGA2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000256|PIRNR:PIRNR016636};
DE            EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR016636};
GN   ORFNames=FC64_GL000589 {ECO:0000313|EMBL:KRM53306.1};
OS   Ligilactobacillus araffinosus DSM 20653.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423820 {ECO:0000313|EMBL:KRM53306.1, ECO:0000313|Proteomes:UP000051291};
RN   [1] {ECO:0000313|EMBL:KRM53306.1, ECO:0000313|Proteomes:UP000051291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20653 {ECO:0000313|EMBL:KRM53306.1,
RC   ECO:0000313|Proteomes:UP000051291};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRM53306.1}.
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DR   EMBL; AYYZ01000004; KRM53306.1; -; Genomic_DNA.
DR   RefSeq; WP_057906085.1; NZ_AYYZ01000004.1.
DR   AlphaFoldDB; A0A0R1ZGA2; -.
DR   STRING; 1423820.FC64_GL000589; -.
DR   PATRIC; fig|1423820.4.peg.596; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000051291; 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   Reference proteome {ECO:0000313|Proteomes:UP000051291};
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        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   399 AA;  47610 MW;  FC898F584A000120 CRC64;
     MINIQPYQNP EYFILLIIGL LPIMIGLLYG RRFRTYETLI SIAFLVLTFG GVKWHQGIAL
     IGYVIFELLL IAWYFNYRQK HNKSWVFCLA VILAIVPLVI VKLTPLFDFN KESIFGFLGI
     SYLTFKVVGM IMEIRDGMIK EFHPWTTLQF IIFFPTISSG PIDRYRRFKE DYDNIPDREK
     YVRMLEKAVH YLFLGFMYKF VLAYFFGQYL MPKVDALAIA HGGWSVWVFL HGYVYAMDLF
     FDFAGYSLFA VATSYVMGIE TPMNFNKPWI SYNVKDFWNR WHMTLSFWFR DYIYMRLVFF
     MMKKKWLKSR IAMANIGYLT LFLIMGFWHG ETWYYIAYGL FQAIAMIVCD AWQRFKKKHR
     EMIPHNKFTE AFAIFLTFNV MCFSLLIFSG FLNTIFVVH
//
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