ACP_AQUAE
ID ACP_AQUAE Reviewed; 78 AA.
AC O67611;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=aq_1716.1;
GN ORFNames=aq_1717A;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07567.1; -; Genomic_DNA.
DR PIR; A70448; A70448.
DR RefSeq; NP_214177.1; NC_000918.1.
DR RefSeq; WP_010881114.1; NC_000918.1.
DR PDB; 2EHS; X-ray; 1.30 A; A=2-78.
DR PDB; 2EHT; X-ray; 1.40 A; A=2-78.
DR PDBsum; 2EHS; -.
DR PDBsum; 2EHT; -.
DR AlphaFoldDB; O67611; -.
DR SMR; O67611; -.
DR STRING; 224324.aq_1717a; -.
DR EnsemblBacteria; AAC07567; AAC07567; aq_1717a.
DR KEGG; aae:aq_1717a; -.
DR PATRIC; fig|224324.8.peg.1318; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_1_0; -.
DR InParanoid; O67611; -.
DR OMA; CEIPDEQ; -.
DR OrthoDB; 1943389at2; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; O67611; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..78
FT /note="Acyl carrier protein"
FT /id="PRO_0000180094"
FT DOMAIN 1..76
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 36
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:2EHS"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2EHS"
FT TURN 28..32
FT /evidence="ECO:0007829|PDB:2EHS"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:2EHS"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:2EHS"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:2EHS"
SQ SEQUENCE 78 AA; 8711 MW; 21E3B7D77157EB35 CRC64;
MSLEERVKEI IAEQLGVEKE KITPEAKFVE DLGADSLDVV ELIMAFEEEF GIEIPDEDAE
KIQTVGDVIN YLKEKVGG