GenomeNet

Database: UniProt
Entry: S2YMW1_9STAP
LinkDB: S2YMW1_9STAP
Original site: S2YMW1_9STAP 
ID   S2YMW1_9STAP            Unreviewed;        78 AA.
AC   S2YMW1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=HMPREF1208_00415 {ECO:0000313|EMBL:EPD53079.1};
OS   Staphylococcus sp. HGB0015.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1078083 {ECO:0000313|EMBL:EPD53079.1, ECO:0000313|Proteomes:UP000014407};
RN   [1] {ECO:0000313|EMBL:EPD53079.1, ECO:0000313|Proteomes:UP000014407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGB0015 {ECO:0000313|EMBL:EPD53079.1,
RC   ECO:0000313|Proteomes:UP000014407};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Staphylococcus sp. HGB0015.";
RL   Submitted (APR-2013) 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:EPD53079.1}.
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; AGEO01000003; EPD53079.1; -; Genomic_DNA.
DR   RefSeq; WP_016424680.1; NZ_KE150417.1.
DR   AlphaFoldDB; S2YMW1; -.
DR   GeneID; 64046918; -.
DR   PATRIC; fig|1078083.3.peg.413; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_19_0_9; -.
DR   UniPathway; UPA00556; -.
DR   Proteomes; UP000014407; 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:EPD53079.1};
KW   Phosphopantetheine {ECO:0000256|HAMAP-Rule:MF_00565};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00565};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014407}.
FT   DOMAIN          1..78
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   MOD_RES         36
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00565"
SQ   SEQUENCE   78 AA;  8982 MW;  C9BD3BB72798CBBE CRC64;
     MDFNEKVLDI IAEVAEDDVV KTNPDIQLFD EGIMDSLQSV QLLVAFQEEL DIEVSIMDFN
     REDWATPNQI INELAKLR
//
DBGET integrated database retrieval system