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Database: UniProt
Entry: A0A2Z4U9N7_9FIRM
LinkDB: A0A2Z4U9N7_9FIRM
Original site: A0A2Z4U9N7_9FIRM 
ID   A0A2Z4U9N7_9FIRM        Unreviewed;        77 AA.
AC   A0A2Z4U9N7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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:AWY97756.1};
GN   ORFNames=DQQ01_05895 {ECO:0000313|EMBL:AWY97756.1};
OS   Blautia argi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1912897 {ECO:0000313|EMBL:AWY97756.1, ECO:0000313|Proteomes:UP000250003};
RN   [1] {ECO:0000313|Proteomes:UP000250003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 15426 {ECO:0000313|Proteomes:UP000250003};
RA   Chang Y.-H., Paek J., Shin Y.;
RT   "Description of Blautia argi sp. nov., a new anaerobic isolated from dog
RT   feces.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; CP030280; AWY97756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4U9N7; -.
DR   KEGG; blau:DQQ01_05895; -.
DR   OrthoDB; 9804551at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000250003; 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:UP000250003}.
FT   DOMAIN          1..74
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   MOD_RES         34
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01217"
SQ   SEQUENCE   77 AA;  8734 MW;  0EABA42FB87FD788 CRC64;
     MLEKMREIIA EQLNCEAESI QMETSFKEDL GADSLDLFEL VMALEDEYSI EIPSEELQDL
     TTVGSVVEYL KSKGVEE
//
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