ID   ACP_STACT               Reviewed;          77 AA.
AC   B9DPJ1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Sca_0855;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}.
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. {ECO:0000255|HAMAP-Rule:MF_01217}.
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; AM295250; CAL27765.1; -; Genomic_DNA.
DR   RefSeq; WP_002480667.1; NC_012121.1.
DR   AlphaFoldDB; B9DPJ1; -.
DR   SMR; B9DPJ1; -.
DR   STRING; 396513.SCA_0855; -.
DR   GeneID; 60545447; -.
DR   GeneID; 62693290; -.
DR   KEGG; sca:SCA_0855; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_1_9; -.
DR   OMA; CEIPDEQ; -.
DR   OrthoDB; 1943389at2; -.
DR   BioCyc; SCAR396513:SCA_RS04325-MON; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000444; 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   TIGRFAMs; TIGR00517; acyl_carrier; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..77
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_1000164802"
FT   DOMAIN          1..76
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         36
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   77 AA;  8562 MW;  50B45828EE5BB839 CRC64;
     MENFDKVKDI IVDRLGVDAD KVTEDASFKD DLGADSLDIA ELVMELEDEF GTEIPDEEAE
     KINTVGDAVN FINNLEK