DLTB_STRT2
ID DLTB_STRT2 Reviewed; 415 AA.
AC Q5M4V4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:30283133};
GN Name=dltB {ECO:0000303|PubMed:30283133};
GN OrderedLocusNames=stu0762 {ECO:0000312|EMBL:AAV60453.1};
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
RN [2] {ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH, ECO:0007744|PDB:6BUI}
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH DLTC, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF 305-VAL-ILE-306
RP AND VAL-305.
RX PubMed=30283133; DOI=10.1038/s41586-018-0568-2;
RA Ma D., Wang Z., Merrikh C.N., Lang K.S., Lu P., Li X., Merrikh H., Rao Z.,
RA Xu W.;
RT "Crystal structure of a membrane-bound O-acyltransferase.";
RL Nature 562:286-290(2018).
CC -!- FUNCTION: O-acyltransferase that catalyzes D-alanylation of both
CC teichoic acid and lipoteichoic acid (LTA) (PubMed:30283133). D-
CC alanylation of LTA plays an important role in modulating the properties
CC of the cell wall in Gram-positive bacteria, influencing the net charge
CC of the cell wall (PubMed:30283133). Catalyzes D-alanylation from DltC
CC carrier protein (PubMed:30283133). {ECO:0000269|PubMed:30283133}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000269|PubMed:30283133}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30283133};
CC Multi-pass membrane protein {ECO:0000269|PubMed:30283133}.
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 (PubMed:30283133). The conserved catalytic
CC His residue is located at the bottom of this funnel and is connected to
CC the intracellular DltC through a narrow tunnel (PubMed:30283133).
CC {ECO:0000269|PubMed:30283133}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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; CP000023; AAV60453.1; -; Genomic_DNA.
DR RefSeq; WP_002950436.1; NC_006448.1.
DR PDB; 6BUG; X-ray; 3.27 A; C/D/F/G=1-415.
DR PDB; 6BUH; X-ray; 3.15 A; C/D/F/H=1-415.
DR PDB; 6BUI; X-ray; 3.27 A; A/B/C/D=1-415.
DR PDBsum; 6BUG; -.
DR PDBsum; 6BUH; -.
DR PDBsum; 6BUI; -.
DR AlphaFoldDB; Q5M4V4; -.
DR SMR; Q5M4V4; -.
DR STRING; 264199.stu0762; -.
DR EnsemblBacteria; AAV60453; AAV60453; stu0762.
DR GeneID; 66898660; -.
DR KEGG; stl:stu0762; -.
DR PATRIC; fig|264199.4.peg.770; -.
DR eggNOG; COG1696; Bacteria.
DR HOGENOM; CLU_025255_2_0_9; -.
DR OMA; CYSMYLF; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000001170; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell membrane; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Teichoic acid D-alanyltransferase"
FT /id="PRO_0000450783"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 37..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 41..56
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 57..60
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 61..87
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 88..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 91..115
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 116..125
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 126..142
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 143..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT INTRAMEM 150..179
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 180..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 184..227
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 228..232
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 233..264
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 265..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT INTRAMEM 275..311
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 312..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 317..336
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 337..339
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 340..373
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 374..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30283133"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0007744|PDB:6BUG, ECO:0007744|PDB:6BUH,
FT ECO:0007744|PDB:6BUI"
FT TOPO_DOM 405..415
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30283133"
FT ACT_SITE 336
FT /evidence="ECO:0000269|PubMed:30283133"
FT MUTAGEN 305..306
FT /note="VI->DD: Reduced binding to DltC."
FT /evidence="ECO:0000269|PubMed:30283133"
FT MUTAGEN 305
FT /note="V->D: Reduced binding to DltC."
FT /evidence="ECO:0000269|PubMed:30283133"
FT HELIX 2..7
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:6BUH"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 41..56
FT /evidence="ECO:0007829|PDB:6BUH"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 63..87
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 91..114
FT /evidence="ECO:0007829|PDB:6BUH"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:6BUH"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 184..206
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:6BUH"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 233..263
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6BUH"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:6BUH"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 317..336
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 340..372
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 382..403
FT /evidence="ECO:0007829|PDB:6BUH"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:6BUH"
SQ SEQUENCE 415 AA; 48794 MW; 836BCC9FFACD4241 CRC64;
MIDFLKQLPH LEPYGNPFYF IYLGIALLPI FIGLFFKKRF AIYECLVSIT FIVLALTGTH
ASQILALLFY IVWQIIWVYS YKRYRSQRDN KWVFYLHSFL VVLPLILVKV EPTINGTQSL
LNFLGISYLT FRAVGMIIEM RDGVLKEFTL GEFLRFMLFM PTFTSGPIDR FKRFNEDYQS
IPNRDELLNM LEQAVKYIML GFLYKFVLAQ IFGSMLLPPL KAQALSQGGI FNLPTLGVMY
VYGFDLFFDF AGYSMFALAV SNLMGIKSPI NFDKPFISRD MKEFWNRWHM SLSFWFRDFV
FMRLVIVLMR NKVFKNRNTT SNVAYIINMM VMGFWHGITW YYIAYGIFHG IGLVINDAWL
RKKKTINKDR KKAGLKPLPE NKWTKALGIF ITFNTVMLSF LIFSGFLNDL WFTKK
