ID   ACP_SACEN               Reviewed;          95 AA.
AC   P11830; A4FH76;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217};
DE            Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217};
GN   Name=acpP {ECO:0000255|HAMAP-Rule:MF_01217}; OrderedLocusNames=SACE_4132;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHOSPHOPANTETHEINYLATION AT SER-39.
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=2066335; DOI=10.1128/jb.173.14.4379-4385.1991;
RA   Revill W.P., Leadlay P.F.;
RT   "Cloning, characterization, and high-level expression in Escherichia coli
RT   of the Saccharopolyspora erythraea gene encoding an acyl carrier protein
RT   potentially involved in fatty acid biosynthesis.";
RL   J. Bacteriol. 173:4379-4385(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-46, AND PHOSPHOPANTETHEINYLATION AT SER-39.
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=3315744; DOI=10.1016/0014-5793(87)80436-2;
RA   Hale R.S., Jordan K.N., Leadlay P.F.;
RT   "A small, discrete acyl carrier protein is involved in de novo fatty acid
RT   biosynthesis in Streptomyces erythraeus.";
RL   FEBS Lett. 224:133-136(1987).
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; M64477; AAA26476.1; -; Genomic_DNA.
DR   EMBL; AM420293; CAM03401.1; -; Genomic_DNA.
DR   PIR; A47030; A47030.
DR   RefSeq; WP_011874252.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; P11830; -.
DR   SMR; P11830; -.
DR   STRING; 405948.SACE_4132; -.
DR   EnsemblBacteria; CAM03401; CAM03401; SACE_4132.
DR   KEGG; sen:SACE_4132; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_4_11; -.
DR   OMA; MFFEDEF; -.
DR   OrthoDB; 1943389at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
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   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..95
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000180181"
FT   DOMAIN          4..79
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         39
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:2066335, ECO:0000269|PubMed:3315744"
SQ   SEQUENCE   95 AA;  10423 MW;  A2D1C4ADC2D94898 CRC64;
     MDRKEIFERI EQVLAEQLGI PAEQITEEAD LREDLGMDSL DLVELVSALE DEVGMRVEQS
     QLEGIETVGH VMELTLDLVA RLATASAADK PEAAS