ID   ACPXL_RHIEC             Reviewed;          92 AA.
AC   P0A2W4; O88153; P24901; Q2K7D1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Acyl carrier protein AcpXL;
DE   AltName: Full=ORF*;
GN   Name=acpXL; OrderedLocusNames=RHE_CH02478;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE3;
RX   PubMed=11717256; DOI=10.1128/jb.183.24.6999-7006.2001;
RA   Lopez O., Morera C., Miranda-Rios J., Girard L., Romero D., Soberon M.;
RT   "Regulation of gene expression in response to oxygen in Rhizobium etli:
RT   role of FnrN in fixNOQP expression and in symbiotic nitrogen fixation.";
RL   J. Bacteriol. 183:6999-7006(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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 (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC91255.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF083916; AAC34462.1; -; Genomic_DNA.
DR   EMBL; CP000133; ABC91255.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003540486.1; NC_007761.1.
DR   AlphaFoldDB; P0A2W4; -.
DR   SMR; P0A2W4; -.
DR   STRING; 347834.RHE_CH02478; -.
DR   EnsemblBacteria; ABC91255; ABC91255; RHE_CH02478.
DR   GeneID; 58689954; -.
DR   GeneID; 61480893; -.
DR   GeneID; 67483197; -.
DR   KEGG; ret:RHE_CH02478; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_2234373_0_0_5; -.
DR   UniPathway; UPA00360; -.
DR   Proteomes; UP000001936; Chromosome.
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   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..92
FT                   /note="Acyl carrier protein AcpXL"
FT                   /id="PRO_0000180239"
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"
SQ   SEQUENCE   92 AA;  10278 MW;  EED7819237FE613E CRC64;
     MTATFDKVAD IIAETSEIDR ATITPESHTI DDLGIDSLDF LDIVFAIDKE FGIKIPLEKW
     TQEVNEGKVS TEEYFVLKNL CAKIDELKAA KA