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ACPXL_RHILO
ID   ACPXL_RHILO             Reviewed;          93 AA.
AC   Q98L53;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Acyl carrier protein AcpXL;
GN   Name=acpXL; OrderedLocusNames=mlr1174;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB48610.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000012; BAB48610.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010909964.1; NC_002678.2.
DR   AlphaFoldDB; Q98L53; -.
DR   SMR; Q98L53; -.
DR   STRING; 266835.14021999; -.
DR   EnsemblBacteria; BAB48610; BAB48610; BAB48610.
DR   GeneID; 66683627; -.
DR   KEGG; mlo:mlr1174; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_3315926_0_0_5; -.
DR   OrthoDB; 1943389at2; -.
DR   UniPathway; UPA00360; -.
DR   Proteomes; UP000000552; 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.
FT   CHAIN           1..93
FT                   /note="Acyl carrier protein AcpXL"
FT                   /id="PRO_0000180240"
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;  10242 MW;  C7623EA0D33BEF1D CRC64;
     MSTTFDKVAK IIADTSEIDI DTITPESHTI DDLGIDSLDF LDIVFAIDKE FGIKVPLEKW
     TQEVNDGKAS TDDYFVMKNL CAKIDALVAA KTA
 
 
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