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Database: UniProt
Entry: A0A221MDS0_9BACI
LinkDB: A0A221MDS0_9BACI
Original site: A0A221MDS0_9BACI 
ID   A0A221MDS0_9BACI        Unreviewed;        78 AA.
AC   A0A221MDS0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_01217, ECO:0000256|RuleBase:RU003545};
DE            Short=ACP {ECO:0000256|HAMAP-Rule:MF_01217};
GN   Name=acpP {ECO:0000256|HAMAP-Rule:MF_01217,
GN   ECO:0000313|EMBL:ASN05774.1};
GN   ORFNames=CFK40_12520 {ECO:0000313|EMBL:ASN05774.1};
OS   Virgibacillus necropolis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN05774.1, ECO:0000313|Proteomes:UP000204391};
RN   [1] {ECO:0000313|EMBL:ASN05774.1, ECO:0000313|Proteomes:UP000204391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN05774.1,
RC   ECO:0000313|Proteomes:UP000204391};
RX   PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA   Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA   Rodriguez-Diaz M., Swings J., De Vos P.;
RT   "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT   Virgibacillus picturae sp. nov., three novel species isolated from
RT   deteriorated mural paintings, transfer of the species of the genus
RT   salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT   Virgibacillus salexigens comb. nov., and emended description of the genus
RT   Virgibacillus.";
RL   Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01217,
CC       ECO:0000256|RuleBase:RU003545}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_01217, ECO:0000256|RuleBase:RU003545}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01217}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-ACP by acpS. {ECO:0000256|RuleBase:RU003545}.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000256|HAMAP-Rule:MF_01217}.
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DR   EMBL; CP022437; ASN05774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221MDS0; -.
DR   KEGG; vne:CFK40_12520; -.
DR   OrthoDB; 9804551at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000204391; 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; ACP-like; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR003231; ACP.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR00517; acyl_carrier; 1.
DR   PANTHER; PTHR20863; ACYL CARRIER PROTEIN; 1.
DR   PANTHER; PTHR20863:SF77; ACYL CARRIER PROTEIN; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Phosphopantetheine {ECO:0000256|HAMAP-Rule:MF_01217,
KW   ECO:0000256|RuleBase:RU003545};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204391}.
FT   DOMAIN          2..77
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   MOD_RES         37
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01217"
SQ   SEQUENCE   78 AA;  8888 MW;  EE9082F6F029EA70 CRC64;
     MADVFDRVKE LIVERLEVEE SKVTMEASFK EDLDADSLDV VELVMELEDE FDMEIADEEA
     EKINTVGDAV NYINSIKS
//
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