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MBTL_MYCBO
ID   MBTL_MYCBO              Reviewed;          84 AA.
AC   P63453; A0A1R3XY30; Q11014; X2BHN6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Acyl carrier protein MbtL;
DE            Short=ACP;
DE   AltName: Full=Mycobactin synthase protein L;
GN   Name=mbtL; OrderedLocusNames=BQ2027_MB1379;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Acyl carrier protein involved in the formation of acyl-S-ACP
CC       intermediates within the mycobactin biosynthesis process. The aliphatic
CC       chains carried by ACP are subsequently transferred on to the mycobactin
CC       core by MbtK (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-ACP, leading to the activated holo-ACP form. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIT99982.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIT99982.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_855033.1; NC_002945.3.
DR   AlphaFoldDB; P63453; -.
DR   SMR; P63453; -.
DR   EnsemblBacteria; SIT99982; SIT99982; BQ2027_MB1379.
DR   PATRIC; fig|233413.5.peg.1511; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..84
FT                   /note="Acyl carrier protein MbtL"
FT                   /id="PRO_0000180270"
FT   DOMAIN          6..81
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         41
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   84 AA;  8969 MW;  9B50302AC4A3E82C CRC64;
     MTSSPSTVST TLLSILRDDL NIDLTRVTPD ARLVDDVGLD SVAFAVGMVA IEERLGVALS
     EEELLTCDTV GELEAAIAAK YRDE
 
 
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