ID   ACP_BORBU               Reviewed;          80 AA.
AC   O51647;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 130.
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=BB_0704;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAC67041.1; -; Genomic_DNA.
DR   PIR; G70187; G70187.
DR   RefSeq; NP_212838.1; NC_001318.1.
DR   RefSeq; WP_002656801.1; NC_001318.1.
DR   PDB; 2KWL; NMR; -; A=1-80.
DR   PDBsum; 2KWL; -.
DR   AlphaFoldDB; O51647; -.
DR   BMRB; O51647; -.
DR   SMR; O51647; -.
DR   STRING; 224326.BB_0704; -.
DR   PRIDE; O51647; -.
DR   EnsemblBacteria; AAC67041; AAC67041; BB_0704.
DR   GeneID; 56567513; -.
DR   KEGG; bbu:BB_0704; -.
DR   PATRIC; fig|224326.49.peg.1095; -.
DR   HOGENOM; CLU_108696_5_6_12; -.
DR   OMA; CEIPDEQ; -.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; O51647; -.
DR   Proteomes; UP000001807; 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   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.
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_0000180110"
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:2KWL"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   HELIX           39..53
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   TURN            57..60
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:2KWL"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:2KWL"
SQ   SEQUENCE   80 AA;  9334 MW;  8B7AD6C944C26FAC CRC64;
     MDNDEIFSKV RSIISEQLDK KEDEITTDSR FVEDLNADSL DIYELLYLLE EAFDDKIPEN
     EANEFETVGD VVNFIKKRKG