ACP_BUCCC
ID ACP_BUCCC Reviewed; 80 AA.
AC Q057L2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=BCc_218;
OS Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=372461;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc;
RX PubMed=17038625; DOI=10.1126/science.1130441;
RA Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA Silva F.J., Moya A., Latorre A.;
RT "A small microbial genome: the end of a long symbiotic relationship?";
RL Science 314:312-313(2006).
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; CP000263; ABJ90687.1; -; Genomic_DNA.
DR RefSeq; WP_011672606.1; NC_008513.1.
DR AlphaFoldDB; Q057L2; -.
DR SMR; Q057L2; -.
DR STRING; 372461.BCc_218; -.
DR EnsemblBacteria; ABJ90687; ABJ90687; BCc_218.
DR KEGG; bcc:BCc_218; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_1_6; -.
DR OMA; CEIPDEQ; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000669; 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..80
FT /note="Acyl carrier protein"
FT /id="PRO_1000073120"
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 80 AA; 9635 MW; 3B082658D5ADEB1C CRC64;
MKNINYRVKK IIAKQFQINI KKISLNNNLK NDLKIDSLDF VELIMLLEEE FNIKLFDIEA
EKIKKIKDII PYIKKKKLKE