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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//