DLTC_BACSU
ID DLTC_BACSU Reviewed; 78 AA.
AC P39579;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=BSU38520;
GN ORFNames=ipa-3r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=7797557; DOI=10.1074/jbc.270.26.15598;
RA Perego M., Glaser P., Minutello A., Strauch M.A., Leopold K., Fischer W.;
RT "Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid
RT in Bacillus subtilis. Identification of genes and regulation.";
RL J. Biol. Chem. 270:15598-15606(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS), AND PHOSPHOPANTETHEINYLATION AT
RP SER-36.
RX PubMed=26193422; DOI=10.1016/j.febslet.2015.07.008;
RA Zimmermann S., Pfennig S., Neumann P., Yonus H., Weininger U.,
RA Kovermann M., Balbach J., Stubbs M.T.;
RT "High-resolution structures of the D-alanyl carrier protein (Dcp) DltC from
RT Bacillus subtilis reveal equivalent conformations of apo- and holo-forms.";
RL FEBS Lett. 589:2283-2289(2015).
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 ECO:0000269|PubMed:7797557}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00565, ECO:0000305|PubMed:7797557}.
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 ECO:0000269|PubMed:26193422}.
CC -!- SIMILARITY: Belongs to the DltC family. {ECO:0000255|HAMAP-
CC Rule:MF_00565}.
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DR EMBL; X73124; CAA51559.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15878.1; -; Genomic_DNA.
DR PIR; S39658; S39658.
DR RefSeq; NP_391731.1; NC_000964.3.
DR RefSeq; WP_003227325.1; NZ_JNCM01000034.1.
DR PDB; 4BPF; X-ray; 1.01 A; A=1-78.
DR PDB; 4BPG; X-ray; 2.20 A; A/B=1-78.
DR PDB; 4BPH; X-ray; 1.80 A; A=1-78.
DR PDBsum; 4BPF; -.
DR PDBsum; 4BPG; -.
DR PDBsum; 4BPH; -.
DR AlphaFoldDB; P39579; -.
DR SMR; P39579; -.
DR STRING; 224308.BSU38520; -.
DR TCDB; 2.A.50.2.1; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR jPOST; P39579; -.
DR PaxDb; P39579; -.
DR PRIDE; P39579; -.
DR EnsemblBacteria; CAB15878; CAB15878; BSU_38520.
DR GeneID; 937361; -.
DR KEGG; bsu:BSU38520; -.
DR PATRIC; fig|224308.179.peg.4171; -.
DR eggNOG; COG0236; Bacteria.
DR OMA; DEWNTPN; -.
DR PhylomeDB; P39579; -.
DR BioCyc; BSUB:BSU38520-MON; -.
DR BioCyc; MetaCyc:BSU38520-MON; -.
DR UniPathway; UPA00556; -.
DR PRO; PR:P39579; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Cytoplasm;
KW Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..78
FT /note="D-alanyl carrier protein"
FT /id="PRO_0000213087"
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,
FT ECO:0000269|PubMed:26193422, ECO:0007744|PDB:4BPH"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:4BPF"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:4BPF"
FT TURN 28..32
FT /evidence="ECO:0007829|PDB:4BPF"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:4BPF"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4BPF"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4BPF"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:4BPF"
SQ SEQUENCE 78 AA; 9009 MW; 4A3F51C4A44CE8F6 CRC64;
MDFKQEVLDV LAEVCQDDIV KENPDIEIFE EGLLDSFGTV ELLLAIENRF DILVPITEFD
RDVWNTPNNI VNQLSELK
