ID   ACP_THET8               Reviewed;          80 AA.
AC   Q5SL79;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=TTHA0414;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of the acyl carrier protein from Thermus thermophilus
RT   HB8.";
RL   Submitted (MAY-2006) to the PDB data bank.
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; AP008226; BAD70237.1; -; Genomic_DNA.
DR   RefSeq; WP_008631656.1; NC_006461.1.
DR   RefSeq; YP_143680.1; NC_006461.1.
DR   PDB; 1X3O; X-ray; 1.50 A; A=1-80.
DR   PDBsum; 1X3O; -.
DR   AlphaFoldDB; Q5SL79; -.
DR   SMR; Q5SL79; -.
DR   STRING; 300852.55771796; -.
DR   EnsemblBacteria; BAD70237; BAD70237; BAD70237.
DR   GeneID; 3168477; -.
DR   KEGG; ttj:TTHA0414; -.
DR   PATRIC; fig|300852.9.peg.414; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_1_0; -.
DR   OMA; CEIPDEQ; -.
DR   PhylomeDB; Q5SL79; -.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; Q5SL79; -.
DR   Proteomes; UP000000532; 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; -; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR003231; Acyl_carrier.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR20863; PTHR20863; 1.
DR   Pfam; PF00550; PP-binding; 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..80
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_1000085618"
FT   DOMAIN          4..79
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         39
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   HELIX           3..18
FT                   /evidence="ECO:0007829|PDB:1X3O"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:1X3O"
FT   TURN            31..35
FT                   /evidence="ECO:0007829|PDB:1X3O"
FT   HELIX           39..53
FT                   /evidence="ECO:0007829|PDB:1X3O"
FT   HELIX           59..64
FT                   /evidence="ECO:0007829|PDB:1X3O"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:1X3O"
SQ   SEQUENCE   80 AA;  9014 MW;  20A245402BBFD99D CRC64;
     MTEQEIFEKV KAVIADKLQV EPEKVTLEAR FIEDLGADSL DTVELIMGLE DEFGLEISDE
     EAEKIRTVKD AVEYIKAKLG