ID ACP1_PSEAE Reviewed; 78 AA.
AC O54439;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-NOV-2024, entry version 154.
DE RecName: Full=Acyl carrier protein 1 {ECO:0000255|HAMAP-Rule:MF_01217};
DE Short=ACP 1 {ECO:0000255|HAMAP-Rule:MF_01217};
GN Name=acpP1 {ECO:0000255|HAMAP-Rule:MF_01217}; Synonyms=acpP;
GN OrderedLocusNames=PA2966;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10464226; DOI=10.1128/jb.181.17.5498-5504.1999;
RA Kutchma A.J., Hoang T.T., Schweizer H.P.;
RT "Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene
RT cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme
RT A:ACP transacylase (fabD).";
RL J. Bacteriol. 181:5498-5504(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; U91631; AAB94392.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06354.1; -; Genomic_DNA.
DR PIR; A83276; A83276.
DR PIR; T12021; T12021.
DR RefSeq; NP_251656.1; NC_002516.2.
DR RefSeq; WP_003091135.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; O54439; -.
DR BMRB; O54439; -.
DR SMR; O54439; -.
DR IntAct; O54439; 2.
DR STRING; 208964.PA2966; -.
DR PaxDb; 208964-PA2966; -.
DR DNASU; 879895; -.
DR GeneID; 77220543; -.
DR GeneID; 879895; -.
DR KEGG; pae:PA2966; -.
DR PATRIC; fig|208964.12.peg.3112; -.
DR PseudoCAP; PA2966; -.
DR HOGENOM; CLU_108696_5_1_6; -.
DR InParanoid; O54439; -.
DR OrthoDB; 9804551at2; -.
DR PhylomeDB; O54439; -.
DR BioCyc; PAER208964:G1FZ6-3018-MONOMER; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR FunFam; 1.10.1200.10:FF:000001; Acyl carrier protein; 1.
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; IPR020806; PKS_PP-bd.
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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..78
FT /note="Acyl carrier protein 1"
FT /id="PRO_0000180167"
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"
FT CONFLICT 76
FT /note="H -> P (in Ref. 1; AAB94392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 78 AA; 8741 MW; 77F95B04F25E1348 CRC64;
MSTIEERVKK IVAEQLGVKE EEVTNSASFV EDLGADSLDT VELVMALEEE FETEIPDEKA
EKITTVQEAI DYIVAHQQ
//
