ID   ACP_XANAL               Reviewed;          79 AA.
AC   Q9EZI1;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 97.
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};
OS   Xanthomonas albilineans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=29447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Xa13;
RX   PubMed=11094291; DOI=10.1111/j.1574-6968.2000.tb09414.x;
RA   Huang G., Zhang L., Birch R.G.;
RT   "Characterization of the acyl carrier protein gene and the fab gene locus
RT   in Xanthomonas albilineans.";
RL   FEMS Microbiol. Lett. 193:129-136(2000).
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; AF294440; AAG42370.1; -; Genomic_DNA.
DR   RefSeq; WP_012915156.1; NZ_MDCB01000008.1.
DR   AlphaFoldDB; Q9EZI1; -.
DR   SMR; Q9EZI1; -.
DR   GeneID; 57875942; -.
DR   OMA; CEIPDEQ; -.
DR   UniPathway; UPA00094; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..79
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000180221"
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"
SQ   SEQUENCE   79 AA;  8844 MW;  15F4CF4852EC1548 CRC64;
     MSTIEERVKK IVVEQLGVKE EEVTNSASFV DDLGADSLDT VELVMALEEE FECEIPDEEA
     EKITSVQQAI DYVKVHVKS