ID   ACP_RHILE               Reviewed;          78 AA.
AC   Q9RG22;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Acyl carrier protein AcpP {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   Rhizobium leguminosarum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LPR5045;
RX   PubMed=10784042; DOI=10.1099/00221287-146-4-839;
RA   Lopez-Lara I.M., Geiger O.;
RT   "Expression and purification of four different rhizobial acyl carrier
RT   proteins.";
RL   Microbiology 146:839-849(2000).
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; AF159243; AAF24179.1; -; Genomic_DNA.
DR   RefSeq; WP_003547058.1; NZ_WXXQ01000005.1.
DR   AlphaFoldDB; Q9RG22; -.
DR   SMR; Q9RG22; -.
DR   STRING; 936136.ARRT01000006_gene2586; -.
DR   GeneID; 58688955; -.
DR   GeneID; 61479904; -.
DR   GeneID; 67484744; -.
DR   eggNOG; COG0236; Bacteria.
DR   OMA; CEIPDEQ; -.
DR   OrthoDB; 1943389at2; -.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR20863; PTHR20863; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 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..78
FT                   /note="Acyl carrier protein AcpP"
FT                   /id="PRO_0000180174"
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   78 AA;  8368 MW;  1F8AF26196409ACB CRC64;
     MSDIAERVKK IVIDHLGVDA DKVVESASFI DDLGADSLDT VELVMAFEEE FGVEIPDDAA
     DSILTVGDAV KFIEKAQA