DLTD_STAA8
ID DLTD_STAA8 Reviewed; 391 AA.
AC Q2FZW3;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein DltD;
GN Name=dltD; OrderedLocusNames=SAOUHSC_00872;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=23858088; DOI=10.1099/mic.0.069898-0;
RA Reichmann N.T., Cassona C.P., Gruendling A.;
RT "Revised mechanism of D-alanine incorporation into cell wall polymers in
RT Gram-positive bacteria.";
RL Microbiology 159:1868-1877(2013).
CC -!- FUNCTION: Involved in the D-alanylation of lipoteichoic acid (LTA).
CC Could be responsible for the transfer of DltC-carried D-alanyl groups
CC to cell membrane phosphatidylglycerol (PG), or alternatively of D-
CC alanine residues from D-Ala-undecaprenol phosphate to the
CC poly(glycerophosphate) chains of LTA. D-alanylation of LTA plays an
CC important role in modulating the properties of the cell wall in Gram-
CC positive bacteria, influencing the net charge of the cell wall.
CC {ECO:0000250|UniProtKB:P39578}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000250|UniProtKB:P39578}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23858088};
CC Single-pass type II membrane protein {ECO:0000255}; Extracellular side
CC {ECO:0000269|PubMed:23858088}.
CC -!- SIMILARITY: Belongs to the DltD family. {ECO:0000305}.
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DR EMBL; CP000253; ABD29997.1; -; Genomic_DNA.
DR RefSeq; WP_000769416.1; NZ_LS483365.1.
DR RefSeq; YP_499425.1; NC_007795.1.
DR AlphaFoldDB; Q2FZW3; -.
DR SMR; Q2FZW3; -.
DR STRING; 1280.SAXN108_0930; -.
DR EnsemblBacteria; ABD29997; ABD29997; SAOUHSC_00872.
DR GeneID; 3919219; -.
DR KEGG; sao:SAOUHSC_00872; -.
DR PATRIC; fig|93061.5.peg.792; -.
DR eggNOG; COG3966; Bacteria.
DR HOGENOM; CLU_050505_1_0_9; -.
DR OMA; QMNWEEA; -.
DR BioCyc; MetaCyc:MON-19992; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000008816; 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:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006998; DltD.
DR InterPro; IPR023896; LTA_DltD.
DR PANTHER; PTHR40039; PTHR40039; 1.
DR Pfam; PF04914; DltD; 1.
DR PIRSF; PIRSF021438; DltD; 1.
DR TIGRFAMs; TIGR04092; LTA_DltD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..391
FT /note="Protein DltD"
FT /id="PRO_0000442352"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23858088"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..391
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:23858088"
SQ SEQUENCE 391 AA; 44946 MW; 23DC88D2BAB27030 CRC64;
MKLKPFLPIL ISGAVFIVFL LLPASWFTGL VNEKTVEDNR TSLTDQVLKG TLIQDKLYES
NKYYPIYGSS ELGKDDPFNP AIALNKHNAN KKAFLLGAGG STDLINAVEL ASQYDKLKGK
KLTFIISPQW FTNHGLTNQN FDARMSQTQI NQMFQQKNMS TELKRRYAQR LLQFPHVHNK
EYLKSYAKNP KETKDSYISG FKENQLIKIE AIKSLFAMDK SPLEHVKPAT KPDASWDEMK
QKAVEIGKAD TTSNKFGIRD QYWKLIQESK RKVRRDYEFN VNSPEFQDLE LLVKTMRAAG
ADVQYVSIPS NGVWYDHIGI DKERRQAVYK KIHSTVVDNG GKIYDMTDKD YEKYVISDAV
HIGWKGWVYM DEQIAKHMKG EPQPEVDKPK N