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   27-MAR-2024, entry version 164.
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; Bacillota; 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}.
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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; 224308-BSU15920; -.
DR   EnsemblBacteria; CAB13465; CAB13465; BSU_15920.
DR   GeneID; 83885596; -.
DR   GeneID; 938486; -.
DR   KEGG; bsu:BSU15920; -.
DR   PATRIC; fig|224308.179.peg.1732; -.
DR   eggNOG; COG0236; Bacteria.
DR   InParanoid; P80643; -.
DR   OrthoDB; 9804551at2; -.
DR   PhylomeDB; P80643; -.
DR   BioCyc; BSUB:BSU15920-MONOMER; -.
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; ACP-like; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR003231; ACP.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR00517; acyl_carrier; 1.
DR   PANTHER; PTHR20863; ACYL CARRIER PROTEIN; 1.
DR   PANTHER; PTHR20863:SF77; ACYL CARRIER PROTEIN; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; ACP-like; 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
//