ACP_HELP2
ID ACP_HELP2 Reviewed; 78 AA.
AC B6JLE2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=HPP12_0566;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001217; ACJ07720.1; -; Genomic_DNA.
DR RefSeq; WP_001163091.1; NC_011498.1.
DR PDB; 5H9G; X-ray; 2.60 A; A/B=1-78.
DR PDB; 5H9H; X-ray; 2.50 A; A/B/C=1-78.
DR PDB; 6IHC; X-ray; 2.40 A; G=7-71.
DR PDBsum; 5H9G; -.
DR PDBsum; 5H9H; -.
DR PDBsum; 6IHC; -.
DR AlphaFoldDB; B6JLE2; -.
DR SMR; B6JLE2; -.
DR EnsemblBacteria; ACJ07720; ACJ07720; HPP12_0566.
DR KEGG; hpp:HPP12_0566; -.
DR HOGENOM; CLU_108696_5_1_7; -.
DR OMA; CEIPDEQ; -.
DR OrthoDB; 1943389at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008198; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..78
FT /note="Acyl carrier protein"
FT /id="PRO_1000139032"
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 8..14
FT /evidence="ECO:0007829|PDB:6IHC"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:6IHC"
FT TURN 28..32
FT /evidence="ECO:0007829|PDB:6IHC"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:6IHC"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:6IHC"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:6IHC"
SQ SEQUENCE 78 AA; 8562 MW; B1735877A07AD811 CRC64;
MALFEDIQAV IAEQLNVDAA QVTPEAEFVK DLGADSLDVV ELIMALEEKF GIEIPDEQAE
KIVNVGDVVK YIEDNKLA
