DLTC_STACT
ID DLTC_STACT Reviewed; 78 AA.
AC B9DIY6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Sca_0536;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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}.
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DR EMBL; AM295250; CAL27450.1; -; Genomic_DNA.
DR RefSeq; WP_015899794.1; NC_012121.1.
DR AlphaFoldDB; B9DIY6; -.
DR SMR; B9DIY6; -.
DR STRING; 396513.SCA_0536; -.
DR GeneID; 60545764; -.
DR GeneID; 62693671; -.
DR KEGG; sca:SCA_0536; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_19_0_9; -.
DR OMA; DEWNTPN; -.
DR OrthoDB; 1943389at2; -.
DR BioCyc; SCAR396513:SCA_RS02745-MON; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000000444; 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_1000146795"
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; 8964 MW; DF9B73CFFEB4547B CRC64;
MEFREQVLDL LAEVAENDVV KENPDVEIFE EGIIDSFQTV GLLLEIQNKL GIEVSIMDFD
RDEWATPNKI VEALEELK
