ACP_BACSU
ID ACP_BACSU Reviewed; 77 AA.
AC P80643; P51832;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217};
DE Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217};
GN Name=acpA; Synonyms=acpP; OrderedLocusNames=BSU15920;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP PROTEIN SEQUENCE OF 15-77, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14, AND
RP PHOSPHOPANTETHEINYLATION AT SER-37.
RC STRAIN=168;
RX PubMed=8759840; DOI=10.1128/jb.178.16.4794-4800.1996;
RA Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.;
RT "Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid
RT biosynthesis genes.";
RL J. Bacteriol. 178:4794-4800(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8654983; DOI=10.1016/0378-1119(96)00181-3;
RA Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.;
RT "The effect of Srb, a homologue of the mammalian SRP receptor alpha-
RT subunit, on Bacillus subtilis growth and protein translocation.";
RL Gene 172:17-24(1996).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 1-17.
RX PubMed=8300523; DOI=10.1128/jb.176.3.681-690.1994;
RA Heaton M.P., Neuhaus F.C.;
RT "Role of the D-alanyl carrier protein in the biosynthesis of D-alanyl-
RT lipoteichoic acid.";
RL J. Bacteriol. 176:681-690(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOLO-(ACYL-CARRIER-PROTEIN) IN
RP COMPLEX WITH HOLO-(ACYL-CARRIER-PROTEIN) SYNTHASE.
RX PubMed=10997907; DOI=10.1016/s0969-2126(00)00178-7;
RA Parris K.D., Lin L., Tam A., Mathew R., Hixon J., Stahl M., Fritz C.C.,
RA Seehra J., Somers W.S.;
RT "Crystal structures of substrate binding to Bacillus subtilis holo-(acyl
RT carrier protein) synthase reveal a novel trimeric arrangement of molecules
RT resulting in three active sites.";
RL Structure 8:883-895(2000).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=11525165; DOI=10.1016/s0969-2126(01)00586-x;
RA Xu G.Y., Tam A., Lin L., Hixon J., Fritz C.C., Powers R.;
RT "Solution structure of B. subtilis acyl carrier protein.";
RL Structure 9:277-287(2001).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01217}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01217}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-ACP by AcpS. This modification is essential for activity because
CC fatty acids are bound in thioester linkage to the sulfhydryl of the
CC prosthetic group.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000255|HAMAP-Rule:MF_01217}.
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; U59433; AAC44308.1; -; Genomic_DNA.
DR EMBL; D64116; BAA10975.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13465.1; -; Genomic_DNA.
DR PIR; JC4822; JC4822.
DR PIR; T46634; T46634.
DR RefSeq; NP_389474.1; NC_000964.3.
DR RefSeq; WP_003154310.1; NZ_JNCM01000035.1.
DR PDB; 1F80; X-ray; 2.30 A; D/E/F=2-77.
DR PDB; 1HY8; NMR; -; A=2-77.
DR PDB; 2X2B; X-ray; 2.69 A; A=1-77.
DR PDBsum; 1F80; -.
DR PDBsum; 1HY8; -.
DR PDBsum; 2X2B; -.
DR AlphaFoldDB; P80643; -.
DR BMRB; P80643; -.
DR SMR; P80643; -.
DR IntAct; P80643; 2.
DR STRING; 224308.BSU15920; -.
DR jPOST; P80643; -.
DR PaxDb; P80643; -.
DR PRIDE; P80643; -.
DR EnsemblBacteria; CAB13465; CAB13465; BSU_15920.
DR GeneID; 64303483; -.
DR GeneID; 66326419; -.
DR GeneID; 938486; -.
DR KEGG; bsu:BSU15920; -.
DR PATRIC; fig|224308.179.peg.1732; -.
DR eggNOG; COG0236; Bacteria.
DR InParanoid; P80643; -.
DR OMA; CEIPDEQ; -.
DR PhylomeDB; P80643; -.
DR BioCyc; BSUB:BSU15920-MON; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P80643; -.
DR PRO; PR:P80643; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003231; Acyl_carrier.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR20863; PTHR20863; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR00517; acyl_carrier; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..77
FT /note="Acyl carrier protein"
FT /id="PRO_0000180104"
FT DOMAIN 2..77
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 37
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:8759840"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:1F80"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2X2B"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1HY8"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:1F80"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:1F80"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1F80"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1F80"
SQ SEQUENCE 77 AA; 8591 MW; 75E745DE3C6A0951 CRC64;
MADTLERVTK IIVDRLGVDE ADVKLEASFK EDLGADSLDV VELVMELEDE FDMEISDEDA
EKIATVGDAV NYIQNQQ
