ID A0A0R1KZB9_9LACO Unreviewed; 402 AA.
AC A0A0R1KZB9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000256|PIRNR:PIRNR016636};
DE EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR016636};
GN ORFNames=FC99_GL002227 {ECO:0000313|EMBL:KRK85745.1};
OS Levilactobacillus koreensis JCM 16448.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423819 {ECO:0000313|EMBL:KRK85745.1, ECO:0000313|Proteomes:UP000050910};
RN [1] {ECO:0000313|EMBL:KRK85745.1, ECO:0000313|Proteomes:UP000050910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16448 {ECO:0000313|EMBL:KRK85745.1,
RC ECO:0000313|Proteomes:UP000050910};
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:KRK85745.1}.
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DR EMBL; AZDP01000123; KRK85745.1; -; Genomic_DNA.
DR RefSeq; WP_048735934.1; NZ_AZDP01000123.1.
DR AlphaFoldDB; A0A0R1KZB9; -.
DR STRING; 637971.ABN16_12010; -.
DR PATRIC; fig|1423819.3.peg.2390; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000050910; 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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 402 AA; 47113 MW; A29089CE7E513689 CRC64;
MLTFEPYGNP TYFALLGVAL LPLMIGLLYG KRSRLYETLI SIFFLVLTFG GSKWTQGVAL
IIYILYEVGL TWGYAVYRRH KNSGPFFYLM VILAIAPLTI VKVTPAVENG QASLIGFLGI
SYLTFRAVQT IMETRDGTLK NYNLMTFLQF MLFFPTISSG PIDRYRRFEK DYRSVPSREQ
YLGMLQKGIR YIFVGFLYKF VLAYYFGTML MPKLQLMAMH SRGGFMDLSW PVVGYMYAYS
ADLFFDFAGY SLFAVGTSYI MGIATPMNFN QPWRSPNIKD FWNRWHITLS FWFRDFIYMR
LVFWFMKHKI FKKPTTTANV TYIINMLVMG FWHGVTWYYI AYGLFHGVAL MVNDMWLRYK
KKHRKSIPHN GFTQIFAIFL TANLVCFSFL IFSGLLNKLW FN
//
