ID ACP_LACLA Reviewed; 73 AA.
AC Q9CHF9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-NOV-2024, entry version 114.
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}; Synonyms=acpA;
GN OrderedLocusNames=LL0772; ORFNames=L0183;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK04870.1; -; Genomic_DNA.
DR PIR; D86721; D86721.
DR RefSeq; NP_266928.1; NC_002662.1.
DR RefSeq; WP_003132501.1; NC_002662.1.
DR AlphaFoldDB; Q9CHF9; -.
DR SMR; Q9CHF9; -.
DR PaxDb; 272623-L0183; -.
DR EnsemblBacteria; AAK04870; AAK04870; L0183.
DR GeneID; 89632905; -.
DR KEGG; lla:L0183; -.
DR PATRIC; fig|272623.7.peg.827; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_0_9; -.
DR OrthoDB; 9804551at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002196; 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; 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 Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..73
FT /note="Acyl carrier protein"
FT /id="PRO_0000180146"
FT DOMAIN 1..73
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 35
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 73 AA; 8401 MW; 89DA432C94B6AB58 CRC64;
MAVFEKVQDI IVDELGKEKE EVTLETSFEE LDADSLDLFQ IINDIEDEFD VEVDTEADMK
TVADLVKYVE NNK
//