ID   ACP_LEPIN               Reviewed;          77 AA.
AC   Q8EXX4;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=LB_083;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010301; AAN51642.1; -; Genomic_DNA.
DR   RefSeq; NP_714627.1; NC_004343.2.
DR   RefSeq; WP_000753030.1; NC_004343.2.
DR   AlphaFoldDB; Q8EXX4; -.
DR   SMR; Q8EXX4; -.
DR   STRING; 189518.LB_083; -.
DR   EnsemblBacteria; AAN51642; AAN51642; LB_083.
DR   GeneID; 61173552; -.
DR   KEGG; lil:LB_083; -.
DR   PATRIC; fig|189518.3.peg.4411; -.
DR   HOGENOM; CLU_108696_5_1_12; -.
DR   InParanoid; Q8EXX4; -.
DR   OMA; CEIPDEQ; -.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:Q8EXX4; -.
DR   Proteomes; UP000001408; Chromosome II.
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: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; 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   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..77
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000180148"
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"
SQ   SEQUENCE   77 AA;  8502 MW;  9C42029B4AED8222 CRC64;
     MADFEKVKSI IVEQLGVDES EVTPEAHFID DLGADSLDTV ELVMALEEEF GIEISDEDAE
     KIQTVGDVTK FIDNLKS