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Database: UniProt
Entry: D8EWG9_9DELT
LinkDB: D8EWG9_9DELT
Original site: D8EWG9_9DELT 
ID   D8EWG9_9DELT            Unreviewed;        78 AA.
AC   D8EWG9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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:EFK12129.1};
GN   ORFNames=NPH_5310 {ECO:0000313|EMBL:EFK12129.1};
OS   delta proteobacterium NaphS2.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK12129.1, ECO:0000313|Proteomes:UP000003834};
RN   [1] {ECO:0000313|EMBL:EFK12129.1, ECO:0000313|Proteomes:UP000003834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NaphS2 {ECO:0000313|EMBL:EFK12129.1,
RC   ECO:0000313|Proteomes:UP000003834};
RX   PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA   Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA   Lipton M.S., Deboy R., Methe B.A.;
RT   "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT   Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL   PLoS ONE 5:E14072-E14072(2010).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFK12129.1}.
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DR   EMBL; ADZZ01000034; EFK12129.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8EWG9; -.
DR   OrthoDB; 9804551at2; -.
DR   UniPathway; UPA00094; -.
DR   UniPathway; UPA00360; -.
DR   Proteomes; UP000003834; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR006162; Ppantetheine_attach_site.
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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_01217}; Reference proteome {ECO:0000313|Proteomes:UP000003834}.
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;  8529 MW;  2C6BA21BEA80C09C CRC64;
     MSTVDEKIVK IICEQLDVPE KDVVPKASFV DDLGADSLDQ VELIMAMEEE FDVSIPDEDA
     EKIATVKDAI DYVKAAVG
//
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