ID   ACPXL_BRUME             Reviewed;          93 AA.
AC   P63450; Q8YGP7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Acyl carrier protein AcpXL;
GN   Name=acpXL; OrderedLocusNames=BMEI1111;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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 (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}.
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DR   EMBL; AE008917; AAL52292.1; -; Genomic_DNA.
DR   PIR; AI3390; AI3390.
DR   RefSeq; WP_002963985.1; NZ_GG703778.1.
DR   AlphaFoldDB; P63450; -.
DR   SMR; P63450; -.
DR   STRING; 224914.BMEI1111; -.
DR   EnsemblBacteria; AAL52292; AAL52292; BMEI1111.
DR   GeneID; 45124282; -.
DR   GeneID; 55590561; -.
DR   KEGG; bme:BMEI1111; -.
DR   PATRIC; fig|224914.52.peg.312; -.
DR   eggNOG; COG0236; Bacteria.
DR   OMA; ATEEYFV; -.
DR   UniPathway; UPA00360; -.
DR   Proteomes; UP000000419; Chromosome I.
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.
FT   CHAIN           1..93
FT                   /note="Acyl carrier protein AcpXL"
FT                   /id="PRO_0000180237"
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   93 AA;  10361 MW;  3383710AADA51807 CRC64;
     MSSTFDKVAD IIAETSEIDR DTITPESHTI DDLGIDSLDF LDIVFAIDKA FGIKIPLEQW
     TQEVNEGKVP TEEYFVLKNL CAKIDELVAA KKG