ID A0A1Q2D8I3_9ENTE Unreviewed; 81 AA.
AC A0A1Q2D8I3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_01217};
DE Short=ACP {ECO:0000256|HAMAP-Rule:MF_01217};
GN Name=acpP {ECO:0000256|HAMAP-Rule:MF_01217};
GN ORFNames=BW732_11325 {ECO:0000313|EMBL:AQP54738.1}, CBF34_04230
GN {ECO:0000313|EMBL:RSU05394.1};
OS Vagococcus penaei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=633807 {ECO:0000313|EMBL:AQP54738.1, ECO:0000313|Proteomes:UP000188246};
RN [1] {ECO:0000313|EMBL:AQP54738.1, ECO:0000313|Proteomes:UP000188246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP54738.1,
RC ECO:0000313|Proteomes:UP000188246};
RX PubMed=19897618; DOI=10.1099/ijs.0.012872-0;
RA Jaffres E., Prevost H., Rossero A., Joffraud J.J., Dousset X.;
RT "Vagococcus penaei sp. nov., isolated from spoilage microbiota of cooked
RT shrimp (Penaeus vannamei).";
RL Int. J. Syst. Evol. Microbiol. 60:2159-2164(2010).
RN [2] {ECO:0000313|EMBL:AQP54738.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP54738.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RSU05394.1, ECO:0000313|Proteomes:UP000286995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24833 {ECO:0000313|EMBL:RSU05394.1,
RC ECO:0000313|Proteomes:UP000286995};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01217}.
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 -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000256|HAMAP-Rule:MF_01217}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019609; AQP54738.1; -; Genomic_DNA.
DR EMBL; NGJV01000006; RSU05394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2D8I3; -.
DR STRING; 633807.BW732_11325; -.
DR KEGG; vpi:BW732_11325; -.
DR OrthoDB; 9804551at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000188246; Chromosome.
DR Proteomes; UP000286995; Unassembled WGS sequence.
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 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 Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01217};
KW Reference proteome {ECO:0000313|Proteomes:UP000188246}.
FT DOMAIN 1..77
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT MOD_RES 36
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01217"
SQ SEQUENCE 81 AA; 9461 MW; 85D1FF03715CC7EF CRC64;
MSTFVKIQEI IVDQLGKEEE EVQLTTNFRE ELEADSLDLF QIMNDIEDAF EEYDVKIETD
EGLTTVEDLV KFVDQQIAEK K
//
