ID   ACP_MARMM               Reviewed;          78 AA.
AC   Q0AQC8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Mmar10_1216;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) 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; CP000449; ABI65509.1; -; Genomic_DNA.
DR   RefSeq; WP_011643156.1; NC_008347.1.
DR   AlphaFoldDB; Q0AQC8; -.
DR   SMR; Q0AQC8; -.
DR   STRING; 394221.Mmar10_1216; -.
DR   EnsemblBacteria; ABI65509; ABI65509; Mmar10_1216.
DR   KEGG; mmr:Mmar10_1216; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_1_5; -.
DR   OMA; CEIPDEQ; -.
DR   OrthoDB; 1943389at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001964; 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   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..78
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_1000066637"
FT   DOMAIN          2..77
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         37
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   78 AA;  8622 MW;  0CEBA1E495716A8D CRC64;
     MSDVLERVSK IVIEHLDVEA EKVTDKASFI DDLGADSLDN VELVMAFEEE FDIEIPDDAA
     EHIQTVGDAV KFISEKVG