DLTC_STAAM
ID DLTC_STAAM Reviewed; 78 AA.
AC P0A018; Q53663;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=D-alanyl carrier protein {ECO:0000255|HAMAP-Rule:MF_00565};
DE Short=DCP {ECO:0000255|HAMAP-Rule:MF_00565};
DE AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00565};
GN Name=dltC {ECO:0000255|HAMAP-Rule:MF_00565}; OrderedLocusNames=SAV0934;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
CC -!- FUNCTION: Carrier protein involved in the D-alanylation of lipoteichoic
CC acid (LTA). The loading of thioester-linked D-alanine onto DltC is
CC catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-
CC carried D-alanyl group is further transferred to cell membrane
CC phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed
CC by DltD. D-alanylation of LTA plays an important role in modulating the
CC properties of the cell wall in Gram-positive bacteria, influencing the
CC net charge of the cell wall. {ECO:0000255|HAMAP-Rule:MF_00565}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00565}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00565}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-DCP. {ECO:0000255|HAMAP-Rule:MF_00565}.
CC -!- SIMILARITY: Belongs to the DltC family. {ECO:0000255|HAMAP-
CC Rule:MF_00565}.
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; BA000017; BAB57096.1; -; Genomic_DNA.
DR RefSeq; WP_000395692.1; NC_002758.2.
DR AlphaFoldDB; P0A018; -.
DR SMR; P0A018; -.
DR PaxDb; P0A018; -.
DR EnsemblBacteria; BAB57096; BAB57096; SAV0934.
DR GeneID; 66839132; -.
DR KEGG; sav:SAV0934; -.
DR HOGENOM; CLU_108696_19_0_9; -.
DR OMA; DEWNTPN; -.
DR PhylomeDB; P0A018; -.
DR BioCyc; SAUR158878:SAV_RS05085-MON; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036370; F:D-alanyl carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_00565; DltC; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003230; DltC.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR01688; dltC; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Cytoplasm; Phosphopantetheine;
KW Phosphoprotein.
FT CHAIN 1..78
FT /note="D-alanyl carrier protein"
FT /id="PRO_0000213098"
FT DOMAIN 1..78
FT /note="Carrier"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
FT MOD_RES 36
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00565"
SQ SEQUENCE 78 AA; 9063 MW; C001D1D3D189A584 CRC64;
MEFREQVLNL LAEVAENDIV KENPDVEIFE EGIIDSFQTV GLLLEIQNKL DIEVSIMDFD
RDEWATPNKI VEALEELR