DLTB_LACRH
ID DLTB_LACRH Reviewed; 405 AA.
AC P35855;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000250|UniProtKB:Q5M4V4};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5M4V4};
DE AltName: Full=Basic membrane protein;
DE Short=BMP;
GN Name=dltB {ECO:0000303|PubMed:9158726};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC / NCIMB 6375 / NCTC 12953;
RX PubMed=9158726; DOI=10.1089/mdr.1996.2.77;
RA Neuhaus F.C., Heaton M.P., Debabov D.V., Zhang Q.;
RT "The dlt operon in the biosynthesis of D-alanyl-lipoteichoic acid in
RT Lactobacillus casei.";
RL Microb. Drug Resist. 2:77-84(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RC STRAIN=ATCC 7469 / DSM 20021 / JCM 1136 / CCUG 21452 / KCTC 1046 / NCDO 243
RC / NCIMB 6375 / NCTC 12953;
RX PubMed=1385594; DOI=10.1128/jb.174.14.4707-4717.1992;
RA Heaton M.P., Neuhaus F.C.;
RT "Biosynthesis of D-alanyl-lipoteichoic acid: cloning, nucleotide sequence,
RT and expression of the Lactobacillus casei gene for the D-alanine-activating
RT enzyme.";
RL J. Bacteriol. 174:4707-4717(1992).
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:0000250|UniProtKB:Q5M4V4}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q5M4V4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5M4V4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5M4V4}.
CC -!- DOMAIN: Consists of a ring of transmembrane domains, which shield a
CC highly conserved extracellular structural funnel extending into the
CC middle of the lipid bilayer. The conserved catalytic His residue is
CC located at the bottom of this funnel and is connected to the
CC intracellular DltC through a narrow tunnel.
CC {ECO:0000250|UniProtKB:Q5M4V4}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U43894; AAB17658.1; -; Genomic_DNA.
DR EMBL; M83993; AAA25235.1; -; Genomic_DNA.
DR PIR; B42983; B42983.
DR AlphaFoldDB; P35855; -.
DR SMR; P35855; -.
DR STRING; 568703.LGG_00778; -.
DR eggNOG; COG1696; Bacteria.
DR UniPathway; UPA00556; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-UniPathway.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR024024; DltB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
DR PIRSF; PIRSF500216; DltB; 1.
DR TIGRFAMs; TIGR04091; LTA_dltB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell membrane; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..405
FT /note="Teichoic acid D-alanyltransferase"
FT /id="PRO_0000213129"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..29
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 30..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..49
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 50..53
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..80
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..111
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 112..121
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..138
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 139..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 146..175
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 176..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..223
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 224..232
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..264
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 265..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 275..310
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 311..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 336..338
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 339..372
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 373..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..405
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT ACT_SITE 335
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
SQ SEQUENCE 405 AA; 47758 MW; 78A05BC980936F63 CRC64;
MLNLQPYENP QYFVYLIIAL LPVIIGMFKG FRMHWYESIF SLVFLVLIFD ADKWPQGKAL
LGYVVFNLLL VYAYFKYRTR EGSKNSTAVF YLSVALGIAH VAVVKFTPLF QHHGSILGFL
GISYLTFRVV GTIMEIRDGS IKDLNMWKFI QFLLFFPTIS SGPIDRYRRF VKDYDRVPDP
EHYAQLVTKA IHYLMLGFLY KFILGYIFGT LWLPSVEHMA MASRGGAFLG LSWPVVGVMY
AYSGYLFFDF AGYSLFAVAI SYLMGIETPM NFNKPWSHIT SRLLNRWQLS LSFWFRDYIY
MRFVFFMMKH KWIKSRVWTA FVGYLVLFLI MGIWHGETWY YIVYGLFHAM LINLTDAWLR
FKKKHKDFFP HNRATHYPSP FSMTANAVCF SFLIFSGFLD KLWFH
