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ACP_MARN8
ID   ACP_MARN8               Reviewed;          77 AA.
AC   A1U1S9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Maqu_1866;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18948.1; -; Genomic_DNA.
DR   RefSeq; WP_008938713.1; NC_008740.1.
DR   AlphaFoldDB; A1U1S9; -.
DR   SMR; A1U1S9; -.
DR   STRING; 351348.Maqu_1866; -.
DR   EnsemblBacteria; ABM18948; ABM18948; Maqu_1866.
DR   KEGG; maq:Maqu_1866; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_1_6; -.
DR   OMA; CEIPDEQ; -.
DR   OrthoDB; 1943389at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000998; 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   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..77
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_1000066636"
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   77 AA;  8561 MW;  4E428FA1C3C648B6 CRC64;
     MSTVEERVKK IVCEQLGVKE SEVQNTSSFV EDLGADSLDT VELVMALEEE FETEIPDEEA
     EKLGTVQDAI DYIVAHT
 
 
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