ID H0E9T0_9ACTN Unreviewed; 83 AA.
AC H0E9T0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_01217};
DE Short=ACP {ECO:0000256|HAMAP-Rule:MF_01217};
GN Name=acpP {ECO:0000256|HAMAP-Rule:MF_01217};
GN ORFNames=PAI11_36020 {ECO:0000313|EMBL:EHN09579.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN09579.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN09579.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN09579.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01217}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01217}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01217}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000256|ARBA:ARBA00010930, ECO:0000256|HAMAP-Rule:MF_01217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN09579.1}.
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DR EMBL; AGUD01000267; EHN09579.1; -; Genomic_DNA.
DR RefSeq; WP_007577855.1; NZ_AGUD01000267.1.
DR AlphaFoldDB; H0E9T0; -.
DR PATRIC; fig|1097667.3.peg.3571; -.
DR OrthoDB; 3186649at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217};
KW Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217};
KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01217};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01217};
KW Phosphopantetheine {ECO:0000256|HAMAP-Rule:MF_01217};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01217};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143}.
FT DOMAIN 4..79
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT MOD_RES 39
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01217"
SQ SEQUENCE 83 AA; 9183 MW; FAF9EC4944323457 CRC64;
MTRDEVFDIV RRHLADELEV DPDSITEGTR LREDLEADSL DLFTLVQELD DTHGVQLPED
EAATITTVGE AVDAVLRHLP AAA
//
