ID ACP_GEOKA Reviewed; 77 AA.
AC Q5L0Q4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-NOV-2024, entry version 101.
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=GK1191;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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}.
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DR EMBL; BA000043; BAD75476.1; -; Genomic_DNA.
DR RefSeq; WP_011230691.1; NC_006510.1.
DR AlphaFoldDB; Q5L0Q4; -.
DR SMR; Q5L0Q4; -.
DR STRING; 235909.GK1191; -.
DR KEGG; gka:GK1191; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_3_9; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0000035; F:acyl binding; IEA:TreeGrafter.
DR GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:TreeGrafter.
DR FunFam; 1.10.1200.10:FF:000001; Acyl carrier protein; 1.
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 InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR00517; acyl_carrier; 1.
DR PANTHER; PTHR20863; ACYL CARRIER PROTEIN; 1.
DR PANTHER; PTHR20863:SF77; ACYL CARRIER PROTEIN; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 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;
KW Reference proteome.
FT CHAIN 1..77
FT /note="Acyl carrier protein"
FT /id="PRO_1000066611"
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 77 AA; 8619 MW; C47CC8C7BCF4BA4C CRC64;
MADVLERVTK IIVDRLGVDE SQVTLEASFK DDLGADSLDI VELVMELEDE FNMEISDEEA
EKIVTVGDAV NYIKSRL
//
