ID   ACP2_PSEAE              Reviewed;          79 AA.
AC   O52658;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Acyl carrier protein 2 {ECO:0000255|HAMAP-Rule:MF_01217};
DE            Short=ACP 2 {ECO:0000255|HAMAP-Rule:MF_01217};
GN   Name=acpP2 {ECO:0000255|HAMAP-Rule:MF_01217}; OrderedLocusNames=PA1869;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K;
RX   PubMed=9680212; DOI=10.1046/j.1365-2958.1998.00888.x;
RA   Martinez A., Ostrovsky P., Nunn D.N.;
RT   "Identification of an additional member of the secretin superfamily of
RT   proteins in Pseudomonas aeruginosa that is able to function in type II
RT   protein secretion.";
RL   Mol. Microbiol. 28:1235-1246(1998).
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; AF044261; AAC38778.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG05258.1; -; Genomic_DNA.
DR   PIR; D83411; D83411.
DR   RefSeq; NP_250560.1; NC_002516.2.
DR   RefSeq; WP_003106681.1; NZ_QZGE01000003.1.
DR   AlphaFoldDB; O52658; -.
DR   BMRB; O52658; -.
DR   SMR; O52658; -.
DR   IntAct; O52658; 2.
DR   STRING; 287.DR97_6; -.
DR   PaxDb; O52658; -.
DR   DNASU; 881955; -.
DR   EnsemblBacteria; AAG05258; AAG05258; PA1869.
DR   GeneID; 881955; -.
DR   KEGG; pae:PA1869; -.
DR   PATRIC; fig|208964.12.peg.1946; -.
DR   PseudoCAP; PA1869; -.
DR   HOGENOM; CLU_108696_5_1_6; -.
DR   InParanoid; O52658; -.
DR   OMA; ATPCMAV; -.
DR   PhylomeDB; O52658; -.
DR   BioCyc; PAER208964:G1FZ6-1909-MON; -.
DR   UniPathway; UPA00094; -.
DR   PHI-base; PHI:8556; -.
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   Gene3D; 1.10.1200.10; -; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR003231; Acyl_carrier.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR20863; PTHR20863; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR00517; acyl_carrier; 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   CHAIN           1..79
FT                   /note="Acyl carrier protein 2"
FT                   /id="PRO_0000180168"
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"
SQ   SEQUENCE   79 AA;  8951 MW;  A7D384788CE81ABA CRC64;
     MDDIETRVRK LVAARFGVEE CDIRLDSDFR NDFGAESLEV VELVMALEAE FGVEIADDDA
     ERIETVRQAI DYLEEAVPT