ID A0A371ARR3_9FIRM Unreviewed; 76 AA.
AC A0A371ARR3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=D-alanyl carrier protein {ECO:0000256|HAMAP-Rule:MF_00565};
DE Short=DCP {ECO:0000256|HAMAP-Rule:MF_00565};
DE AltName: Full=D-alanine--poly(phosphoribitol) ligase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00565};
GN Name=dltC {ECO:0000256|HAMAP-Rule:MF_00565};
GN ORFNames=DWV06_17275 {ECO:0000313|EMBL:RDU22269.1};
OS Anaerosacchariphilus polymeriproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosacchariphilus.
OX NCBI_TaxID=1812858 {ECO:0000313|EMBL:RDU22269.1, ECO:0000313|Proteomes:UP000255036};
RN [1] {ECO:0000313|EMBL:RDU22269.1, ECO:0000313|Proteomes:UP000255036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCWD5 {ECO:0000313|EMBL:RDU22269.1,
RC ECO:0000313|Proteomes:UP000255036};
RA Kim W., Yang S.-H., Oh J., Lee J.-H., Kwon K.K.;
RT "Anaerosacharophilus polymeroproducens gen. nov. sp. nov., an anaerobic
RT bacterium isolated from salt field.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00565}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00565}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00565}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-DCP. {ECO:0000256|HAMAP-Rule:MF_00565}.
CC -!- SIMILARITY: Belongs to the DltC family. {ECO:0000256|HAMAP-
CC Rule:MF_00565}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDU22269.1}.
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DR EMBL; QRCT01000050; RDU22269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371ARR3; -.
DR OrthoDB; 6462171at2; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000255036; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036370; F:D-alanyl carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; ACP-like; 1.
DR HAMAP; MF_00565; DltC; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003230; DltC.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01688; dltC; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00565};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00565};
KW Ligase {ECO:0000313|EMBL:RDU22269.1};
KW Phosphopantetheine {ECO:0000256|HAMAP-Rule:MF_00565};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00565};
KW Reference proteome {ECO:0000313|Proteomes:UP000255036}.
FT DOMAIN 1..76
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT MOD_RES 34
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00565"
SQ SEQUENCE 76 AA; 8601 MW; 36FFF442397CCC94 CRC64;
MEKELLELLE KVCEDSIVKE DLDVELFESD LLDSLGFAEL LAEIELTFGV FISPSEIERS
EINTPNKIIA MIKARS
//
