ID   ACPXL_RHILV             Reviewed;          92 AA.
AC   P0A2W5; O88153; P24901;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Acyl carrier protein AcpXL;
GN   Name=acpXL;
OS   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28; 30-41 AND
RP   69-75, CHARACTERIZATION, PHOSPHOPANTETHEINYLATION AT SER-37, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=VF39;
RX   PubMed=8943266; DOI=10.1074/jbc.271.50.32126;
RA   Brozek K.A., Carlson R.W., Raetz C.R.H.;
RT   "A special acyl carrier protein for transferring long hydroxylated fatty
RT   acids to lipid A in Rhizobium.";
RL   J. Biol. Chem. 271:32126-32136(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Basu S.S., Karbarz M.J., Raetz C.R.H.;
RT   "Expression cloning and characterization of the C28 acyltransferase of
RT   lipid A biosynthesis in Rhizobium leguminosarum acyl chain incorporation
RT   into Rhizobium leguminosarum lipid A.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51, AND PHOSPHOPANTETHEINYLATION AT
RP   SER-37.
RC   STRAIN=VF39;
RX   PubMed=2175385; DOI=10.1007/bf00315806;
RA   Colonna-Romano S., Arnold W., Schlueter A., Boistard P., Puehler A.,
RA   Priefer U.B.;
RT   "An Fnr-like protein encoded in Rhizobium leguminosarum biovar viciae shows
RT   structural and functional homology to Rhizobium meliloti FixK.";
RL   Mol. Gen. Genet. 223:138-147(1990).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis. Is involved in the transfer of long hydroxylated fatty
CC       acids to lipid A. Is acylated predominantly with 27-hydroxyoctacosanoic
CC       acid.
CC   -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
CC   -!- MASS SPECTROMETRY: Mass=10486.0; Method=Electrospray; Note=Isoform
CC       derivatized with 4'-phosphopantetheine.;
CC       Evidence={ECO:0000269|PubMed:8943266};
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM44294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA39311.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF081835; AAC32203.1; -; Genomic_DNA.
DR   EMBL; AF510733; AAM44294.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X55788; CAA39311.1; ALT_INIT; Genomic_DNA.
DR   PIR; S11950; S11950.
DR   RefSeq; WP_003540486.1; NZ_SJNN01000046.1.
DR   AlphaFoldDB; P0A2W5; -.
DR   SMR; P0A2W5; -.
DR   GeneID; 58689954; -.
DR   GeneID; 61480893; -.
DR   GeneID; 67483197; -.
DR   UniPathway; UPA00360; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR003231; Acyl_carrier.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR20863; PTHR20863; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Phosphopantetheine; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8943266"
FT   CHAIN           2..92
FT                   /note="Acyl carrier protein AcpXL"
FT                   /id="PRO_0000180241"
FT   DOMAIN          2..88
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                   ECO:0000269|PubMed:2175385, ECO:0000269|PubMed:8943266"
SQ   SEQUENCE   92 AA;  10278 MW;  EED7819237FE613E CRC64;
     MTATFDKVAD IIAETSEIDR ATITPESHTI DDLGIDSLDF LDIVFAIDKE FGIKIPLEKW
     TQEVNEGKVS TEEYFVLKNL CAKIDELKAA KA